{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P52769","uniProtkbId":"ACCD_PINTH","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-11-24","entryVersion":98,"sequenceVersion":2},"annotationScore":4.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"ACCase subunit beta"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Acetyl-CoA carboxylase carboxyltransferase subunit beta"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"2.1.3.15"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"accD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)-biotinyl-L-lysyl-[protein] + malonyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54728"},{"database":"Rhea","id":"RHEA-COMP:10505"},{"database":"Rhea","id":"RHEA-COMP:10506"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:83144"},{"database":"ChEBI","id":"CHEBI:83145"}],"ecNumber":"2.1.3.15","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Plastid, chloroplast stroma","id":"SL-0055"}}]},{"commentType":"RNA EDITING","locationType":"Known","positions":[{"position":"88","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11078738"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Belongs to the AccD/PCCB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic","featureId":"PRO_0000199792"},{"type":"Domain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"CoA carboxyltransferase N-terminal","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01136"}]},{"type":"Zinc finger","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}]},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0691","category":"Coding sequence diversity","name":"RNA editing"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"},{"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"11078738","citationType":"journal article","authors":["Sasaki Y.","Kozaki A.","Ohmori A.","Iguchi H.","Nagano Y."],"citationCrossReferences":[{"database":"PubMed","id":"11078738"},{"database":"DOI","id":"10.1074/jbc.m008166200"}],"title":"Chloroplast RNA editing required for functional acetyl-CoA carboxylase in plants.","publicationDate":"2001","journal":"J. Biol. Chem.","firstPage":"3937","lastPage":"3940","volume":"276"},"referencePositions":["RNA EDITING"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04367.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07489","properties":[{"key":"EntryName","value":"T07489"}]},{"database":"RefSeq","id":"NP_042410.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P52769","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P52769","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809073","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00655","properties":[{"key":"RectionId","value":"UER00711"}]},{"database":"GO","id":"GO:0009317","properties":[{"key":"GoTerm","value":"C:acetyl-CoA carboxylase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009570","properties":[{"key":"GoTerm","value":"C:chloroplast stroma"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003989","properties":[{"key":"GoTerm","value":"F:acetyl-CoA carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016743","properties":[{"key":"GoTerm","value":"F:carboxyl- or carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:2001295","properties":[{"key":"GoTerm","value":"P:malonyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01395","properties":[{"key":"EntryName","value":"AcetylCoA_CT_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034733","properties":[{"key":"EntryName","value":"AcCoA_carboxyl_beta"}]},{"database":"InterPro","id":"IPR000438","properties":[{"key":"EntryName","value":"Acetyl_CoA_COase_Trfase_b_su"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR011762","properties":[{"key":"EntryName","value":"COA_CT_N"}]},{"database":"NCBIfam","id":"TIGR00515","properties":[{"key":"EntryName","value":"accD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42995","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42995:SF5","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01039","properties":[{"key":"EntryName","value":"Carboxyl_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01070","properties":[{"key":"EntryName","value":"ACCCTRFRASEB"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50980","properties":[{"key":"EntryName","value":"COA_CT_NTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIKEWFEDKRKITALLKNSVERDSKDANETEKNKNKSIDYAKIKKLWAQCDNCENLLYLRFLRENQSVCKECGYYLQMNSSDRIELLIDRDTWRPMDEDMYTLDVLQFYSENEPSHSDNLNSEDESYKDHITFYQIETGLTDAIQTGIGQLNGLTIALGVMDFQFMGGSMGSVVGEKITRLIERATAESLPLIMVCASGGARMQEGSFSLMQMAKIASALYIHQKEKKLLYISILTSPTTGGVTASFGMLGDIIIAEPKAYIAFAGKRVIEQTLGQKVIEDFQVTEHLFGHGLFDLIVPRNLLKGVLSELFWFYVLRSSL","length":321,"molWeight":36403,"crc64":"7AAC0BBE6315980A","md5":"9B60EFC151B3EE40AACF0ADBCF97322E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"RNA EDITING":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Zinc finger":1,"Binding site":4},"uniParcId":"UPI0001BBE3FD"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P69551","secondaryAccessions":["P24684"],"uniProtkbId":"PSBA_PINTH","entryAudit":{"firstPublicDate":"2005-03-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":97,"sequenceVersion":2},"annotationScore":4.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II protein D1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII D1 protein"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"1.10.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II Q(B) protein"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"psbA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 a plastoquinone + 4 hnu + 2 H2O = 2 a plastoquinol + O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36359"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:62192"}],"ecNumber":"1.10.3.9","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"value":"Belongs to the reaction center PufL/M/PsbA/D family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Photosystem II protein D1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_0000090465"},{"type":"Propeptide","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"featureId":"PRO_0000316477"},{"type":"Transmembrane","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Transmembrane","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"ChlzD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:136840"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"pheophytin a","id":"ChEBI:CHEBI:136840","label":"D1"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"PD1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"a quinone","id":"ChEBI:CHEBI:132124","label":"B"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Tyrosine radical intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Stabilizes free radical intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Cleavage; by CTPA","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylthreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01379"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0106","category":"Ligand","name":"Calcium"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0359","category":"Biological process","name":"Herbicide resistance"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"1557027","citationType":"journal article","authors":["Tsudzuki J.","Nakashima K.","Tsudzuki T.","Hiratsuka J.","Shibata M.","Wakasugi T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"1557027"},{"database":"DOI","id":"10.1007/bf00279998"}],"title":"Chloroplast DNA of black pine retains a residual inverted repeat lacking rRNA genes: nucleotide sequences of trnQ, trnK, psbA, trnI and trnH and the absence of rps16.","publicationDate":"1992","journal":"Mol. Gen. Genet.","firstPage":"206","lastPage":"214","volume":"232"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D11467","properties":[{"key":"ProteinId","value":"BAA02024.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04462.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S29327","properties":[{"key":"EntryName","value":"S29327"}]},{"database":"RefSeq","id":"NP_042347.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P69551","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P69551","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809093","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016168","properties":[{"key":"GoTerm","value":"F:chlorophyll binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010242","properties":[{"key":"GoTerm","value":"F:oxygen evolving activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009772","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd09289","properties":[{"key":"EntryName","value":"Photosystem-II_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.85.10:FF:000002","properties":[{"key":"EntryName","value":"Photosystem II protein D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.85.10","properties":[{"key":"EntryName","value":"Photosystem II protein D1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01379","properties":[{"key":"EntryName","value":"PSII_PsbA_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR055266","properties":[{"key":"EntryName","value":"D1/D2"}]},{"database":"InterPro","id":"IPR036854","properties":[{"key":"EntryName","value":"Photo_II_D1/D2_sf"}]},{"database":"InterPro","id":"IPR000484","properties":[{"key":"EntryName","value":"Photo_RC_L/M"}]},{"database":"InterPro","id":"IPR055265","properties":[{"key":"EntryName","value":"Photo_RC_L/M_CS"}]},{"database":"InterPro","id":"IPR005867","properties":[{"key":"EntryName","value":"PSII_D1"}]},{"database":"NCBIfam","id":"TIGR01151","properties":[{"key":"EntryName","value":"psbA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149:SF12","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II D2 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II PROTEIN D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00124","properties":[{"key":"EntryName","value":"Photo_RC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00256","properties":[{"key":"EntryName","value":"REACTNCENTRE"}]},{"database":"SUPFAM","id":"SSF81483","properties":[{"key":"EntryName","value":"Bacterial photosystem II reaction centre, L and M subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00244","properties":[{"key":"EntryName","value":"REACTION_CENTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAIIERRESANLWSRFCDWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENQSANAGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVAGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVESISIGG","length":353,"molWeight":38808,"crc64":"8F80C298EE1FACA1","md5":"0857B4A6C69E14A0565071C6867F97BF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":2,"MISCELLANEOUS":2,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Propeptide":1,"Transmembrane":5,"Binding site":13,"Site":3,"Modified residue":2},"uniParcId":"UPI00001569E1"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41621","uniProtkbId":"RBL_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":116,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Ribulose bisphosphate carboxylase large chain"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"RuBisCO large subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"4.1.1.39"}]},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"rbcL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO2 + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58272"}],"ecNumber":"4.1.1.39","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-3-phosphoglycerate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36631"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58033"},{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Belongs to the RuBisCO large chain family. Type I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Propeptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"featureId":"PRO_0000031369"},{"type":"Chain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large chain","featureId":"PRO_0000031370"},{"type":"Active site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Active site","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"in homodimeric partner","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":3,"modifier":"EXACT"}},"description":"N-acetylproline","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"N6,N6,N6-trimethyllysine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Disulfide bond","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Interchain; in linked form","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0113","category":"Biological process","name":"Calvin cycle"},{"id":"KW-0120","category":"Biological process","name":"Carbon dioxide fixation"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0488","category":"PTM","name":"Methylation"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0601","category":"Biological process","name":"Photorespiration"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04368.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07490","properties":[{"key":"EntryName","value":"T07490"}]},{"database":"RefSeq","id":"NP_042411.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41621","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41621","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809094","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016984","properties":[{"key":"GoTerm","value":"F:ribulose-bisphosphate carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019253","properties":[{"key":"GoTerm","value":"P:reductive pentose-phosphate cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd08212","properties":[{"key":"EntryName","value":"RuBisCO_large_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.110:FF:000001","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.150:FF:000001","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.110","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase, large subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.150","properties":[{"key":"EntryName","value":"RuBisCO large subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01338","properties":[{"key":"EntryName","value":"RuBisCO_L_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR033966","properties":[{"key":"EntryName","value":"RuBisCO"}]},{"database":"InterPro","id":"IPR020878","properties":[{"key":"EntryName","value":"RuBisCo_large_chain_AS"}]},{"database":"InterPro","id":"IPR000685","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C"}]},{"database":"InterPro","id":"IPR036376","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C_sf"}]},{"database":"InterPro","id":"IPR017443","properties":[{"key":"EntryName","value":"RuBisCO_lsu_fd_N"}]},{"database":"InterPro","id":"IPR036422","properties":[{"key":"EntryName","value":"RuBisCO_lsu_N_sf"}]},{"database":"InterPro","id":"IPR020888","properties":[{"key":"EntryName","value":"RuBisCO_lsuI"}]},{"database":"NCBIfam","id":"NF003252","properties":[{"key":"EntryName","value":"PRK04208.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704:SF15","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00016","properties":[{"key":"EntryName","value":"RuBisCO_large"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02788","properties":[{"key":"EntryName","value":"RuBisCO_large_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01052","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00014","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00301","properties":[{"key":"EntryName","value":"RuBisCO-like_proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51649","properties":[{"key":"EntryName","value":"RuBisCo, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54966","properties":[{"key":"EntryName","value":"RuBisCO, large subunit, small (N-terminal) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00157","properties":[{"key":"EntryName","value":"RUBISCO_LARGE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSPKTETKASVGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEETQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEALNKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQRNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDVTLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREACKWSPELAAACEIWKEIKFEFDVIDRL","length":475,"molWeight":52756,"crc64":"467B25FBA35875F1","md5":"E55D9D4B535607E4075F6C54C881AACC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Propeptide":1,"Chain":1,"Active site":2,"Binding site":9,"Site":1,"Modified residue":3,"Disulfide bond":1},"uniParcId":"UPI0000133326"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41602","uniProtkbId":"ATPA_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":136,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"ATP synthase subunit alpha, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"7.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"ATP synthase F1 sector subunit alpha"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"F-ATPase subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"atpA"}}],"comments":[{"texts":[{"value":"Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"value":"Belongs to the ATPase alpha/beta chains family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"ATP synthase subunit alpha, chloroplastic","featureId":"PRO_0000144389"},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01346"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0139","category":"Cellular component","name":"CF(1)"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04319.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07439","properties":[{"key":"EntryName","value":"T07439"}]},{"database":"RefSeq","id":"NP_042360.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41602","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41602","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"808991","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043531","properties":[{"key":"GoTerm","value":"F:ADP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18113","properties":[{"key":"EntryName","value":"ATP-synt_F1_alpha_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18116","properties":[{"key":"EntryName","value":"ATP-synt_F1_alpha_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01132","properties":[{"key":"EntryName","value":"F1-ATPase_alpha_CD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.150.20:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.20:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000002","properties":[{"key":"EntryName","value":"ATP synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.150.20","properties":[{"key":"EntryName","value":"ATP synthase alpha/beta chain, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01346","properties":[{"key":"EntryName","value":"ATP_synth_alpha_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023366","properties":[{"key":"EntryName","value":"ATP_synth_asu-like_sf"}]},{"database":"InterPro","id":"IPR000793","properties":[{"key":"EntryName","value":"ATP_synth_asu_C"}]},{"database":"InterPro","id":"IPR038376","properties":[{"key":"EntryName","value":"ATP_synth_asu_C_sf"}]},{"database":"InterPro","id":"IPR033732","properties":[{"key":"EntryName","value":"ATP_synth_F1_a_nt-bd_dom"}]},{"database":"InterPro","id":"IPR005294","properties":[{"key":"EntryName","value":"ATP_synth_F1_asu"}]},{"database":"InterPro","id":"IPR020003","properties":[{"key":"EntryName","value":"ATPase_a/bsu_AS"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR036121","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N_sf"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00962","properties":[{"key":"EntryName","value":"atpA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009884","properties":[{"key":"EntryName","value":"PRK13343.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48082","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48082:SF2","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00306","properties":[{"key":"EntryName","value":"ATP-synt_ab_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47917","properties":[{"key":"EntryName","value":"C-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50615","properties":[{"key":"EntryName","value":"N-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00152","properties":[{"key":"EntryName","value":"ATPASE_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGSIRLDEISSIIRKQIEQYNNEVRVGNLGTVLQVGDGIARIHGLDEVMAGELVEFGDGTVGIALNLGSDNVGAVLMGDGLMIQEGSSVRATGKIAQIPVSDAYLGRVVNALAQPIDGKGKISASEFRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKSQNVICVYVAIGQRASSVAQVVNTFRERGAMAYTIVVAETADSPATLQYLAPYTGATLAEYFMYKKQHTSIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSVTALPIVETQAGDVSAYIPTNAISITDGQIFSSADLFNAGIRPAINVGISVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKATQDQLARGQRLRELLKQSQSAPLTVEEQIATIYTGTNGYLDIFEIAQVRKFLLGLRFYLIKNKPQFGEIIRSTGTFTEEAKALLEEAL","length":494,"molWeight":53381,"crc64":"97DCB1DF4265AF23","md5":"4960F8F9AE9E549FB82CE5A0DAAFAC7D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":1,"Site":1},"uniParcId":"UPI0000126406"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41603","uniProtkbId":"ATPH_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":118,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATP synthase subunit c, chloroplastic"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATP synthase F(0) sector subunit c"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"ATPase subunit III"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F-type ATPase subunit c"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F-ATPase subunit c"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Lipid-binding protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"atpH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"value":"In plastids the F-type ATPase is also known as CF(1)CF(0)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}],"value":"Belongs to the ATPase C chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"ATP synthase subunit c, chloroplastic","featureId":"PRO_0000112202"},{"type":"Transmembrane","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}]},{"type":"Transmembrane","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}]},{"type":"Site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01396"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"id":"KW-0138","category":"Cellular component","name":"CF(0)"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04320.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07441","properties":[{"key":"EntryName","value":"T07441"}]},{"database":"RefSeq","id":"NP_042362.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41603","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41603","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809035","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033177","properties":[{"key":"GoTerm","value":"C:proton-transporting two-sector ATPase complex, proton-transporting domain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd18183","properties":[{"key":"EntryName","value":"ATP-synt_Fo_c_ATPH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.20.10:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit c, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.20.10","properties":[{"key":"EntryName","value":"F1F0 ATP synthase subunit C"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01396","properties":[{"key":"EntryName","value":"ATP_synth_c_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005953","properties":[{"key":"EntryName","value":"ATP_synth_csu_bac/chlpt"}]},{"database":"InterPro","id":"IPR000454","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu"}]},{"database":"InterPro","id":"IPR020537","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu_DDCD_BS"}]},{"database":"InterPro","id":"IPR038662","properties":[{"key":"EntryName","value":"ATP_synth_F0_csu_sf"}]},{"database":"InterPro","id":"IPR002379","properties":[{"key":"EntryName","value":"ATPase_proteolipid_c-like_dom"}]},{"database":"InterPro","id":"IPR035921","properties":[{"key":"EntryName","value":"F/V-ATP_Csub_sf"}]},{"database":"NCBIfam","id":"TIGR01260","properties":[{"key":"EntryName","value":"ATP_synt_c"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF005608","properties":[{"key":"EntryName","value":"PRK07354.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10031","properties":[{"key":"EntryName","value":"ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10031:SF48","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT C, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00137","properties":[{"key":"EntryName","value":"ATP-synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00124","properties":[{"key":"EntryName","value":"ATPASEC"}]},{"database":"SUPFAM","id":"SSF81333","properties":[{"key":"EntryName","value":"F1F0 ATP synthase subunit C"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00605","properties":[{"key":"EntryName","value":"ATPASE_C"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDPLISAASVIAAGLSVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV","length":81,"molWeight":8007,"crc64":"340DCEC22BF8FFA9","md5":"F156B1BF7256AD3E022B1540C83ED47D"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":2,"Site":1},"uniParcId":"UPI000012659F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41615","uniProtkbId":"PSBE_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2023-11-08","lastSequenceUpdateDate":"2007-01-23","entryVersion":98,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Cytochrome b559 subunit alpha"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"PSII reaction center subunit V"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"psbE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"value":"Belongs to the PsbE/PsbF family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"Cytochrome b559 subunit alpha","featureId":"PRO_0000200332"},{"type":"Transmembrane","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00642"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","note":"ligand shared with beta subunit"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04353.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07475","properties":[{"key":"EntryName","value":"T07475"}]},{"database":"RefSeq","id":"NP_042396.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41615","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41615","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809007","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009539","properties":[{"key":"GoTerm","value":"C:photosystem II reaction center"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009767","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport chain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.5.860","properties":[{"key":"EntryName","value":"Photosystem II cytochrome b559, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00642","properties":[{"key":"EntryName","value":"PSII_PsbE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006217","properties":[{"key":"EntryName","value":"PSII_cyt_b559_asu"}]},{"database":"InterPro","id":"IPR037025","properties":[{"key":"EntryName","value":"PSII_cyt_b559_asu_sf"}]},{"database":"InterPro","id":"IPR006216","properties":[{"key":"EntryName","value":"PSII_cyt_b559_CS"}]},{"database":"InterPro","id":"IPR013081","properties":[{"key":"EntryName","value":"PSII_cyt_b559_N"}]},{"database":"InterPro","id":"IPR013082","properties":[{"key":"EntryName","value":"PSII_cytb559_asu_lum"}]},{"database":"NCBIfam","id":"TIGR01332","properties":[{"key":"EntryName","value":"cyt_b559_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391:SF9","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00283","properties":[{"key":"EntryName","value":"Cytochrom_B559"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00284","properties":[{"key":"EntryName","value":"Cytochrom_B559a"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000036","properties":[{"key":"EntryName","value":"PsbE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161045","properties":[{"key":"EntryName","value":"Cytochrome b559 subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00537","properties":[{"key":"EntryName","value":"CYTOCHROME_B559"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGNTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQEVPLVTGRFDPLEQLDEFTRSF","length":83,"molWeight":9482,"crc64":"DE1FD893E9E5AB24","md5":"0B29560985A64F10D789135963BAD031"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":1,"Binding site":1},"uniParcId":"UPI000016389C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41622","uniProtkbId":"ATPB_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":134,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"ATP synthase subunit beta, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"7.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"ATP synthase F1 sector subunit beta"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"F-ATPase subunit beta"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"atpB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Belongs to the ATPase alpha/beta chains family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"ATP synthase subunit beta, chloroplastic","featureId":"PRO_0000144542"},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0139","category":"Cellular component","name":"CF(1)"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04370.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07492","properties":[{"key":"EntryName","value":"T07492"}]},{"database":"RefSeq","id":"NP_042413.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41622","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41622","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809040","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:GOC"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042776","properties":[{"key":"GoTerm","value":"P:proton motive force-driven mitochondrial ATP synthesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd18110","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18115","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01133","properties":[{"key":"EntryName","value":"F1-ATPase_beta_CD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1140.10:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000004","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.170:FF:000002","properties":[{"key":"EntryName","value":"ATP synthase subunit beta, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.170","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1140.10","properties":[{"key":"EntryName","value":"Bovine Mitochondrial F1-atpase, Atp Synthase Beta Chain, Chain D, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01347","properties":[{"key":"EntryName","value":"ATP_synth_beta_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR055190","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"}]},{"database":"InterPro","id":"IPR005722","properties":[{"key":"EntryName","value":"ATP_synth_F1_bsu"}]},{"database":"InterPro","id":"IPR020003","properties":[{"key":"EntryName","value":"ATPase_a/bsu_AS"}]},{"database":"InterPro","id":"IPR050053","properties":[{"key":"EntryName","value":"ATPase_alpha/beta_chains"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR036121","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N_sf"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR024034","properties":[{"key":"EntryName","value":"ATPase_F1/V1_b/a_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR01039","properties":[{"key":"EntryName","value":"atpD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184","properties":[{"key":"EntryName","value":"ATP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184:SF71","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22919","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47917","properties":[{"key":"EntryName","value":"C-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50615","properties":[{"key":"EntryName","value":"N-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00152","properties":[{"key":"EntryName","value":"ATPASE_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKNPLVLGVSASVETNVGRIAQIIGPVLDVSFPPGNMPNIYNSLIVKGQGTAGQEIQVTCEVQQLLGNHKVRAVAMSATDGLTRGMRVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDAGITSPIHRPAPAFTELDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVIDEQKISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHSDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVGLMETIRGFQMILSGELDGLIEQSFYLVGNIDEATAKAINSSMES","length":492,"molWeight":52747,"crc64":"170B2D32A1A25504","md5":"5EACE63171E0161599858320D9D4BCFA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":1},"uniParcId":"UPI0000126472"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41629","uniProtkbId":"RPOA_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":126,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-directed RNA polymerase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"PEP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Plastid-encoded RNA polymerase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"RNA polymerase subunit alpha"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"rpoA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Belongs to the RNA polymerase alpha chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase subunit alpha","featureId":"PRO_0000175482"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Alpha N-terminal domain (alpha-NTD)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}]},{"type":"Region","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Alpha C-terminal domain (alpha-CTD)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00059"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04395.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07517","properties":[{"key":"EntryName","value":"T07517"}]},{"database":"RefSeq","id":"NP_042438.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41629","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41629","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809011","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046983","properties":[{"key":"GoTerm","value":"F:protein dimerization activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06928","properties":[{"key":"EntryName","value":"RNAP_alpha_NTD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.170.120.12:FF:000001","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.120.12","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase, insert domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.10","properties":[{"key":"EntryName","value":"RNA polymerase, RBP11-like subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00059","properties":[{"key":"EntryName","value":"RNApol_bact_RpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011262","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_insert"}]},{"database":"InterPro","id":"IPR011263","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_RpoA/D/Rpb3"}]},{"database":"InterPro","id":"IPR011773","properties":[{"key":"EntryName","value":"DNA-dir_RpoA"}]},{"database":"InterPro","id":"IPR036603","properties":[{"key":"EntryName","value":"RBP11-like"}]},{"database":"InterPro","id":"IPR011260","properties":[{"key":"EntryName","value":"RNAP_asu_C"}]},{"database":"InterPro","id":"IPR036643","properties":[{"key":"EntryName","value":"RNApol_insert_sf"}]},{"database":"NCBIfam","id":"TIGR02027","properties":[{"key":"EntryName","value":"rpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01000","properties":[{"key":"EntryName","value":"RNA_pol_A_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03118","properties":[{"key":"EntryName","value":"RNA_pol_A_CTD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01193","properties":[{"key":"EntryName","value":"RNA_pol_L"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00662","properties":[{"key":"EntryName","value":"RPOLD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47789","properties":[{"key":"EntryName","value":"C-terminal domain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56553","properties":[{"key":"EntryName","value":"Insert subdomain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55257","properties":[{"key":"EntryName","value":"RBP11-like subunits of RNA polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIRDEISVSIQTLRWKCIESRAYSKRLHYGRFALSPLHKGRADTIGIAMRRALLGEVEGTCITRVKLENIKHEYSAIIGIEESVHDILMNLKEIVFRSDSYGIREASIYIVGPRNVTAQDIILPPSVKIIDTTQHIARLTKSITSDIRLQIEKNRGYIIHSPNNYQDGIFPIDAVFMPVRDANYSIHSYGSGNEIREVLFLEIWTNGGLTPREALYEASRNLIDLFIPFLHGEEQNIDGMNNKKGSNMLPFPLSHVLTDTGETKEKIAFQLIFIDQLELPPKTYNSLRRANIHTLLDLLNYSREDLMRIEHFGKESVEQVLEVLQKLFAIDPPRN","length":335,"molWeight":38355,"crc64":"547753D8AA2E5F3C","md5":"42164726B036A8E1D66A7EDF98ECBD07"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":2},"uniParcId":"UPI00001346A7"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41638","uniProtkbId":"RR4_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1995-11-01","entryVersion":98,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Small ribosomal subunit protein uS4c"}},"alternativeNames":[{"fullName":{"value":"30S ribosomal protein S4, chloroplastic"}}]},"genes":[{"geneName":{"value":"rps4"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"With S5 and S12 plays an important role in translational accuracy"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the universal ribosomal protein uS4 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"Small ribosomal subunit protein uS4c","featureId":"PRO_0000132653"},{"type":"Domain","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"S4 RNA-binding"},{"type":"Region","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"id":"KW-0689","category":"Molecular function","name":"Ribosomal protein"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04412.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07536","properties":[{"key":"EntryName","value":"T07536"}]},{"database":"RefSeq","id":"NP_042457.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41638","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41638","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809000","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0015935","properties":[{"key":"GoTerm","value":"C:small ribosomal subunit"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003735","properties":[{"key":"GoTerm","value":"F:structural constituent of ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042274","properties":[{"key":"GoTerm","value":"P:ribosomal small subunit biogenesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00165","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1050.10:FF:000002","properties":[{"key":"EntryName","value":"30S ribosomal protein S4, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1050.10","properties":[{"key":"EntryName","value":"Ribosomal Protein S4 Delta 41, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.290.10","properties":[{"key":"EntryName","value":"RNA-binding S4 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01306_B","properties":[{"key":"EntryName","value":"Ribosomal_uS4_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022801","properties":[{"key":"EntryName","value":"Ribosomal_uS4"}]},{"database":"InterPro","id":"IPR005709","properties":[{"key":"EntryName","value":"Ribosomal_uS4_bact"}]},{"database":"InterPro","id":"IPR001912","properties":[{"key":"EntryName","value":"Ribosomal_uS4_N"}]},{"database":"InterPro","id":"IPR002942","properties":[{"key":"EntryName","value":"S4_RNA-bd"}]},{"database":"InterPro","id":"IPR036986","properties":[{"key":"EntryName","value":"S4_RNA-bd_sf"}]},{"database":"NCBIfam","id":"NF003717","properties":[{"key":"EntryName","value":"rpsD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11831","properties":[{"key":"EntryName","value":"30S 40S RIBOSOMAL PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11831:SF4","properties":[{"key":"EntryName","value":"SMALL RIBOSOMAL SUBUNIT PROTEIN US4M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00163","properties":[{"key":"EntryName","value":"Ribosomal_S4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01479","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01390","properties":[{"key":"EntryName","value":"Ribosomal_S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00363","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55174","properties":[{"key":"EntryName","value":"Alpha-L RNA-binding motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50889","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRYRGPRLKIIRRLKTLPGLTSKRPKNRKDSMNRSSSRKISQYRIRLEEKQKLRFHYGLTERQLLKYVRIARRAKGSRVRSIAITEMRLDKSFSIGYGSTSGARQLVNHGHIRVNDHMVDIPSYPCKPQDVITIRDQQRLRAIIKKNIDLFQRDKLPNHLTFHSLQYKGFINQIIDSKWINLKINELLVVEYYSRQA","length":198,"molWeight":23488,"crc64":"B8E094D6274E4A81","md5":"CE6A2CB0009B6DC1C7E9A4B6DBD8538B"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":1},"uniParcId":"UPI000013499C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41639","uniProtkbId":"PSAA_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":113,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Photosystem I P700 chlorophyll a apoprotein A1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"PSI-A"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"PsaA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"psaA"}}],"comments":[{"texts":[{"value":"PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"value":"Belongs to the PsaA/PsaB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":753,"modifier":"EXACT"}},"description":"Photosystem I P700 chlorophyll a apoprotein A1","featureId":"PRO_0000088571"},{"type":"Transmembrane","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Helical; Name=I","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Helical; Name=II","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Helical; Name=III","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Helical; Name=IV","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"Helical; Name=V","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"Helical; Name=VI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Helical; Name=VII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":552,"modifier":"EXACT"}},"description":"Helical; Name=VIII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Helical; Name=IX","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":667,"modifier":"EXACT"},"end":{"value":689,"modifier":"EXACT"}},"description":"Helical; Name=X","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Transmembrane","location":{"start":{"value":727,"modifier":"EXACT"},"end":{"value":747,"modifier":"EXACT"}},"description":"Helical; Name=XI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}]},{"type":"Binding site","location":{"start":{"value":576,"modifier":"EXACT"},"end":{"value":576,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":585,"modifier":"EXACT"},"end":{"value":585,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":678,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189419"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a'","id":"ChEBI:CHEBI:189419","label":"A1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":686,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"A3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":694,"modifier":"EXACT"},"end":{"value":694,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"A3"}},{"type":"Binding site","location":{"start":{"value":695,"modifier":"EXACT"},"end":{"value":695,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18067"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00458"}],"ligand":{"name":"phylloquinone","id":"ChEBI:CHEBI:18067","label":"A"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04419.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07543","properties":[{"key":"EntryName","value":"T07543"}]},{"database":"RefSeq","id":"NP_042464.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41639","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41639","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809016","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.1130.10:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I P700 chlorophyll a apoprotein A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1130.10","properties":[{"key":"EntryName","value":"Photosystem I PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00458","properties":[{"key":"EntryName","value":"PSI_PsaA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006243","properties":[{"key":"EntryName","value":"PSI_PsaA"}]},{"database":"InterPro","id":"IPR001280","properties":[{"key":"EntryName","value":"PSI_PsaA/B"}]},{"database":"InterPro","id":"IPR020586","properties":[{"key":"EntryName","value":"PSI_PsaA/B_CS"}]},{"database":"InterPro","id":"IPR036408","properties":[{"key":"EntryName","value":"PSI_PsaA/B_sf"}]},{"database":"NCBIfam","id":"TIGR01335","properties":[{"key":"EntryName","value":"psaA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN, OMPA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128:SF19","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00223","properties":[{"key":"EntryName","value":"PsaA_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002905","properties":[{"key":"EntryName","value":"PSI_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00257","properties":[{"key":"EntryName","value":"PHOTSYSPSAAB"}]},{"database":"SUPFAM","id":"SSF81558","properties":[{"key":"EntryName","value":"Photosystem I subunits PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00419","properties":[{"key":"EntryName","value":"PHOTOSYSTEM_I_PSAAB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIRSPEPEVKKVKVVVDRDTVKTSFEKWAKPGHFSRTLAKGPDTTTWIWNLHADAHDFDSHTNNLEDISRKIFSAHFGQLAIIFIWLSGMYYHGARFSNYEAWLADPTHIKPSAQIVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALIFAALMLFAGWFHYHKAAPKLAWFQEVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINQLLDAGVDPKEIPLPHEFIFNRDLLAQLYPSFAKGVTPFLTLNWSEYSDFLTFRGGLNPVTGGLWLTDTAHHHLAIAVLFLIAGHMYKTNWRIGHNLKDLLEAHKGPFTGEGHKGLYEILTTSWHAQLAVNLAMLGSLTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFIIVGAAAHAAIFMVRDYDPTTQYNNLLDRVLRHRDAIVSHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWIQNTHASAPGSTAPGATASTSLTWGGGDLVTVGSKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGNISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLLFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSIVQGRAVGVAHYLLGGIVTTWAFFLARIIAIG","length":753,"molWeight":83608,"crc64":"CD7ECF10D802DD28","md5":"45C4C33C1C9172B8EF3A1117EDDF0B97"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":11,"Binding site":6},"uniParcId":"UPI0000132490"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q00864","uniProtkbId":"CHLB_PINTH","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-04-01","entryVersion":97,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Light-independent protochlorophyllide reductase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"DPOR subunit B"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"LI-POR subunit B"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"chlB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"value":"Belongs to the ChlB/BchB/BchZ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"Light-independent protochlorophyllide reductase subunit B","featureId":"PRO_0000219839"},{"type":"Active site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}]},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00353"}],"ligand":{"name":"substrate"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"1557027","citationType":"journal article","authors":["Tsudzuki J.","Nakashima K.","Tsudzuki T.","Hiratsuka J.","Shibata M.","Wakasugi T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"1557027"},{"database":"DOI","id":"10.1007/bf00279998"}],"title":"Chloroplast DNA of black pine retains a residual inverted repeat lacking rRNA genes: nucleotide sequences of trnQ, trnK, psbA, trnI and trnH and the absence of rps16.","publicationDate":"1992","journal":"Mol. Gen. Genet.","firstPage":"206","lastPage":"214","volume":"232"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D11467","properties":[{"key":"ProteinId","value":"BAA02020.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04310.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S29324","properties":[{"key":"EntryName","value":"S29324"}]},{"database":"RefSeq","id":"NP_042351.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"Q00864","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q00864","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809089","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01981","properties":[{"key":"EntryName","value":"Pchlide_reductase_B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.89.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1980","properties":[{"key":"EntryName","value":"Nitrogenase molybdenum iron protein domain"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"1.10.8.550","properties":[{"key":"EntryName","value":"Proto-chlorophyllide reductase 57 kD subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00353","properties":[{"key":"EntryName","value":"ChlB_BchB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050152","properties":[{"key":"EntryName","value":"ChlB/BchB/BchZ"}]},{"database":"InterPro","id":"IPR013580","properties":[{"key":"EntryName","value":"LI-POR_suB-like_C"}]},{"database":"InterPro","id":"IPR000510","properties":[{"key":"EntryName","value":"Nase/OxRdtase_comp1"}]},{"database":"InterPro","id":"IPR042298","properties":[{"key":"EntryName","value":"P-CP_red_C"}]},{"database":"InterPro","id":"IPR005969","properties":[{"key":"EntryName","value":"Protochl_reductB"}]},{"database":"InterPro","id":"IPR016209","properties":[{"key":"EntryName","value":"Protochlorophyllide_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01278","properties":[{"key":"EntryName","value":"DPOR_BchB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33712","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33712:SF7","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00148","properties":[{"key":"EntryName","value":"Oxidored_nitro"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08369","properties":[{"key":"EntryName","value":"PCP_red"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000163","properties":[{"key":"EntryName","value":"PCP_ChlB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53807","properties":[{"key":"EntryName","value":"Helical backbone' metal receptor"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLAHWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERNFTPATASIVDRHVLARGSRKRVVDHIIRKDKEEGPDLIILTPTCTSSILQEDLKNFVDRASIISDCNVIFADVDHYQVNEIQAADRTLEQVVRYYLEKSHTLDQFVTDAPSVNIIGILTLGFHNRHDCRELRRLLKDLDIRINQIIPEGGSVEDPKNLPKARFNLIPYREVGLMTAMYLNKEFGMPYVSTTPMGAVDMAECIRQIKKSLETLAAPILSSKRVDYESYIDGQTRFVSQAAWFSRSIDCQNFTGKETVVFGDATHAASITKILAREMGIRVSCTGTYCKHDAEWFKEQIKDFCDEIIITDDHAEVGDIISRVEPSAIFGTQMERHIGKRLEIPCGVISAPAHIQNFSLGYRPFLGYEGTNQIADLVYNSFALGMEDHLLDIFCGHDTKEIMTKSLSTDISPIWDPESRQELGKIPRFVRDEVKRNTEKFARRKGILNVTVEVMHAAKEALS","length":510,"molWeight":57741,"crc64":"45606AC561640D58","md5":"D0F01632600C848305F0C4B716308C51"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":2},"uniParcId":"UPI0000127854"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41640","uniProtkbId":"PSAB_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":114,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Photosystem I P700 chlorophyll a apoprotein A2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PSI-B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"psaB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"value":"Belongs to the PsaA/PsaB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":734,"modifier":"EXACT"}},"description":"Photosystem I P700 chlorophyll a apoprotein A2","featureId":"PRO_0000088633"},{"type":"Transmembrane","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Helical; Name=I","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Helical; Name=II","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Helical; Name=III","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Helical; Name=IV","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Helical; Name=V","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Helical; Name=VI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"Helical; Name=VII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":535,"modifier":"EXACT"}},"description":"Helical; Name=VIII","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"Helical; Name=IX","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":643,"modifier":"EXACT"},"end":{"value":665,"modifier":"EXACT"}},"description":"Helical; Name=X","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Transmembrane","location":{"start":{"value":707,"modifier":"EXACT"},"end":{"value":727,"modifier":"EXACT"}},"description":"Helical; Name=XI","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}]},{"type":"Binding site","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":654,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":662,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"B3"}},{"type":"Binding site","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":671,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18067"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00482"}],"ligand":{"name":"phylloquinone","id":"ChEBI:CHEBI:18067","label":"B"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04420.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07544","properties":[{"key":"EntryName","value":"T07544"}]},{"database":"RefSeq","id":"NP_042465.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41640","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41640","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809085","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009522","properties":[{"key":"GoTerm","value":"C:photosystem I"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.1130.10:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I P700 chlorophyll a apoprotein A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1130.10","properties":[{"key":"EntryName","value":"Photosystem I PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00482","properties":[{"key":"EntryName","value":"PSI_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001280","properties":[{"key":"EntryName","value":"PSI_PsaA/B"}]},{"database":"InterPro","id":"IPR020586","properties":[{"key":"EntryName","value":"PSI_PsaA/B_CS"}]},{"database":"InterPro","id":"IPR036408","properties":[{"key":"EntryName","value":"PSI_PsaA/B_sf"}]},{"database":"InterPro","id":"IPR006244","properties":[{"key":"EntryName","value":"PSI_PsaB"}]},{"database":"NCBIfam","id":"TIGR01336","properties":[{"key":"EntryName","value":"psaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN, OMPA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30128:SF19","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00223","properties":[{"key":"EntryName","value":"PsaA_PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002905","properties":[{"key":"EntryName","value":"PSI_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00257","properties":[{"key":"EntryName","value":"PHOTSYSPSAAB"}]},{"database":"SUPFAM","id":"SSF81558","properties":[{"key":"EntryName","value":"Photosystem I subunits PsaA/PsaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00419","properties":[{"key":"EntryName","value":"PHOTOSYSTEM_I_PSAAB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASRFPKFSQGLAQDPTTRRIWFGIATAHHFESHDDITEERLYHKIFASHFGQLAIIFLWTSGNLFHVAWQGNFEAWVRDPLHVRPIAHAIWDPHFGQPAIEAFTRGGAPGPVNIAYSGVYQWWYTIGLRTNEDLYAGALFLLFLSVIFLIAGRLHLQPKWRPSVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPESRGVHVRWDNFLDVLPHPEGLEPLFTGQWNLYAQNPDSSSHLFGTSQGAGTAILTFLGGFHPQTQSLWLTDMAHHHLAIALVFSIAGHMYRTNFGIGHSMEDILEAHVPPGGLLGRGHKGLYNTINNSLHFQLGLALASLGVITSLVAQHMYSLPPYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFLIRDYNPEQNKDNVLARMLEQKEAIISHLSWVSLLLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTLYGFDILLSSTSGPSFDAGKSIWLPGWLNAINDNNNSLFSTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSRLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVAQFNESSTYLMGWSRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLVRWRDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG","length":734,"molWeight":82485,"crc64":"083720BA7B19266E","md5":"FA5315BA748899F7E50B01755DAE4C08"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":11,"Binding site":6},"uniParcId":"UPI00001324BB"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41649","uniProtkbId":"PSAC_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":112,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Photosystem I iron-sulfur center"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"1.97.1.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"9 kDa polypeptide"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"PSI-C"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Photosystem I subunit VII"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"PsaC"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"psaC"},"synonyms":[{"value":"frxA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30407"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10039"},{"database":"Rhea","id":"RHEA-COMP:10040"},{"database":"ChEBI","id":"CHEBI:29036"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:49552"}],"ecNumber":"1.97.1.12","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"The eukaryotic PSI reaction center is composed of at least 11 subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"value":"Stromal side","id":"SL-9917"}}]}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Photosystem I iron-sulfur center","featureId":"PRO_0000061999"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"4Fe-4S ferredoxin-type 1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}]},{"type":"Domain","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"4Fe-4S ferredoxin-type 2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01303"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0677","category":"Domain","name":"Repeat"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04447.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07571","properties":[{"key":"EntryName","value":"T07571"}]},{"database":"RefSeq","id":"NP_042492.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41649","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41649","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809030","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009522","properties":[{"key":"GoTerm","value":"C:photosystem I"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009773","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem I"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.30.70.20:FF:000001","properties":[{"key":"EntryName","value":"Photosystem I iron-sulfur center"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01303","properties":[{"key":"EntryName","value":"PSI_PsaC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017896","properties":[{"key":"EntryName","value":"4Fe4S_Fe-S-bd"}]},{"database":"InterPro","id":"IPR017900","properties":[{"key":"EntryName","value":"4Fe4S_Fe_S_CS"}]},{"database":"InterPro","id":"IPR050157","properties":[{"key":"EntryName","value":"PSI_iron-sulfur_center"}]},{"database":"InterPro","id":"IPR017491","properties":[{"key":"EntryName","value":"PSI_PsaC"}]},{"database":"NCBIfam","id":"TIGR03048","properties":[{"key":"EntryName","value":"PS_I_psaC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24960:SF79","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I IRON-SULFUR CENTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24960","properties":[{"key":"EntryName","value":"PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14697","properties":[{"key":"EntryName","value":"Fer4_21"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54862","properties":[{"key":"EntryName","value":"4Fe-4S ferredoxins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00198","properties":[{"key":"EntryName","value":"4FE4S_FER_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51379","properties":[{"key":"EntryName","value":"4FE4S_FER_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MAHSVKIYDTCIGCTQCVRACPTDVLEMIPWEGCKAKQIASAPRTEDCAGCKRCESACPTDFLSVRVYLWHETTRSMGLAY","length":81,"molWeight":9008,"crc64":"C907CB61F25603A9","md5":"0E423B79747F99DD42C70AF6A410B019"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":2,"Binding site":8},"uniParcId":"UPI000016389E"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41606","uniProtkbId":"RPOC2_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-10-01","entryVersion":101,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"DNA-directed RNA polymerase subunit beta''"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"PEP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Plastid-encoded RNA polymerase subunit beta''"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"RNA polymerase subunit beta''"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"rpoC2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Binds 1 Zn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"value":"Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1224,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase subunit beta''","featureId":"PRO_0000067942"},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01324"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04325.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07446","properties":[{"key":"EntryName","value":"T07446"}]},{"database":"RefSeq","id":"NP_042367.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41606","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41606","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809025","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02655","properties":[{"key":"EntryName","value":"RNAP_beta'_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.132.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.390","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1790.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.274.100","properties":[{"key":"EntryName","value":"RNA polymerase Rpb1, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01324","properties":[{"key":"EntryName","value":"RNApol_bact_RpoC2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012756","properties":[{"key":"EntryName","value":"DNA-dir_RpoC2_beta_pp"}]},{"database":"InterPro","id":"IPR050254","properties":[{"key":"EntryName","value":"RNA_pol_beta''_euk"}]},{"database":"InterPro","id":"IPR042102","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3_sf"}]},{"database":"InterPro","id":"IPR007083","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"}]},{"database":"InterPro","id":"IPR007081","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"}]},{"database":"InterPro","id":"IPR038120","properties":[{"key":"EntryName","value":"Rpb1_funnel_sf"}]},{"database":"NCBIfam","id":"TIGR02388","properties":[{"key":"EntryName","value":"rpoC2_cyan"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34995","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34995:SF1","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05000","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04998","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_5"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIWRFFLMKERTRLPFDNLPFYNKVMDKTAIKKLISRLIDHFGMTYTSHILDQLKTSGFQQATDTAISLGIDDLLTAPSKGWLVQDAEQQGSVSEKQNHYGNVHAVEKLRQSIEIWYATSEYLRKEMNPNFSMTDPLNPVHVMSFSGARGSTSQVHQLVGMRGLMSDPQGQIIDLPIRRNLREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVVQHIVVRRTDCGTIQGIFVSPIRGRERDRNEIVVRTQILIGRVLADDVYINRRCIATRNQDIGVGLANQLINLRTQPIYIRTPFTCKSISRICQLCYGRSTTHSHLIELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGDIAEHIRAPFNGKIEFNENLVYPTRTRNGHPAYLCHNNLSITIDGQDQVQNLTIPPQSLLLVQNDQYVESEQLIAEVRARTSSFKEKVRKNIYSDLEGEMHWSTNVCHAPEYVQGNVHPILRTGYLWILSGGIYGSRVVPFPFHKYQDQVYVQPFVAKHQSLSDSYVDQVEHRSGDSNCYEKEEQIFSYSETETDRTISNKHRDSIYVFYPNNYNIKGKKQMNRFIVSLQCDKEWEKKIIPCPDAILRIPKSGILQRNSIFGYSNVEHGIPDGSNMTTPFSLDLSREGDNLQIQISYSISYEDGERIQVMSDISIPLVRTCIGFDWEQIDSIESEAYVSLISVRTNKIVNNMVQISLMKYPPFFMGRRDNKTSPNLMFHNNLDHTNLLSSNGASQLISKHQGIICSLSNGEEDSGSFMVLSPSDYFRIVLFNDSKCYDTGNQSNRKDPMRKIIEFSGLLGNLHSITNRFPSSHFLTYKKVLSKKHSIFHNSFNTFQVPKYYFMDENMIIYHFDPCRNIISNLLGPNWCSSSSESEFCEKTFPVVSLGQLIPESVWISEDEPLPESGQIIAVDEESLVIRSAKPYLATRKATVHSHYGKILDKGDTLITLIYERFKSSDIIQGLPKVEQLSEARLNNSISMNLKESFENWTGDMTRFLGSLWGLFISARITMEQSQIHLVNQIQKVYRSQGVRIGDKHIEVIVRQMTSKVLISEDGTANVFSPGELIVLSRAQRMDRALEEAIYYQTMLLGITRASLNTQSFISEASFQETARVLAKAALQGRIDWLKGLKENVILGGMIPAGTGQHIHRSGKRNGIDPRIGNRNLFSNKVKDILFHHDKVDFFSFQDNSYKYHNILKQQLK","length":1224,"molWeight":139272,"crc64":"DCD355D333A4601B","md5":"5CEDC2C0616FDB2F5127E23825B1F86A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":4},"uniParcId":"UPI000013476C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41607","uniProtkbId":"RPOB_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1995-11-01","entryVersion":113,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"DNA-directed RNA polymerase subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"PEP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"Plastid-encoded RNA polymerase subunit beta"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"RNA polymerase subunit beta"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"rpoB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01321"}],"value":"Belongs to the RNA polymerase beta chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1075,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase subunit beta","featureId":"PRO_0000048041"}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04326.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07448","properties":[{"key":"EntryName","value":"T07448"}]},{"database":"RefSeq","id":"NP_042369.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41607","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41607","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809068","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032549","properties":[{"key":"GoTerm","value":"F:ribonucleoside binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00653","properties":[{"key":"EntryName","value":"RNA_pol_B_RPB2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.150","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1100.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.150.10","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase, beta subunit, external 1 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.270.10","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase, subunit 2, domain 6"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1800.10","properties":[{"key":"EntryName","value":"RNA polymerase alpha subunit dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1110.10","properties":[{"key":"EntryName","value":"RNA polymerase Rpb2, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01321","properties":[{"key":"EntryName","value":"RNApol_bact_RpoB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR042107","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_bsu_ext_1_sf"}]},{"database":"InterPro","id":"IPR015712","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_su2"}]},{"database":"InterPro","id":"IPR007120","properties":[{"key":"EntryName","value":"DNA-dir_RNAP_su2_dom"}]},{"database":"InterPro","id":"IPR037033","properties":[{"key":"EntryName","value":"DNA-dir_RNAP_su2_hyb_sf"}]},{"database":"InterPro","id":"IPR010243","properties":[{"key":"EntryName","value":"RNA_pol_bsu_bac"}]},{"database":"InterPro","id":"IPR007121","properties":[{"key":"EntryName","value":"RNA_pol_bsu_CS"}]},{"database":"InterPro","id":"IPR007644","properties":[{"key":"EntryName","value":"RNA_pol_bsu_protrusion"}]},{"database":"InterPro","id":"IPR007642","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_2"}]},{"database":"InterPro","id":"IPR037034","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_2_sf"}]},{"database":"InterPro","id":"IPR007645","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_3"}]},{"database":"InterPro","id":"IPR007641","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_7"}]},{"database":"InterPro","id":"IPR014724","properties":[{"key":"EntryName","value":"RNA_pol_RPB2_OB-fold"}]},{"database":"NCBIfam","id":"NF001616","properties":[{"key":"EntryName","value":"rpoB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20856","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04563","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04561","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04565","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00562","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04560","properties":[{"key":"EntryName","value":"RNA_pol_Rpb2_7"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01166","properties":[{"key":"EntryName","value":"RNA_POL_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRLDENEGAFTIPEFGKIQFEGFCRFIDQGLMEELHNFPKIEDIDKEIEFRLFGNEYELAEPFIKERDAVYQSLTYYSELYVPARSIRRNSRKIQKQTVFLGNIPLMNSHGTFVVNGIYRVVVNQILISPGIYYRSELDHNRINYIYTGTLISDWGRRSKLEIDVGERIWARVSRKQKISIPVLLSAMGLNLEEILDNTRYPERFLFLLKKKGRWEREEYLWSREKAILEFYKKLYCISGDLVFSESLCKELQKKFFRKRCELGKIGRRNLNQKLNLDIPENEIFSLPQDVLAAVDYLIGVKFGMGTLDDIDHLRNRRIRSVADLLQNQFRLALGRLEDAVKRTIRRATKRRSTPQNLVTSTLLKNTFQDFFGSHPLSQFLDQTNPLTEIAHGRKLSHLGPGGLTGRTASFRTRDIHPSYYGRICPIDTSEGMNAGLVASLSIHAKIGDCGSLQSPFYKISERSREEHMVYLLPGEDEDEYYRIATGNSLALNQGIQEEQITPARYRQEFIVIAWEQIHFRSIFPFQYFSVGVSLIPFLEHNDANRALMGSNMQRQAVPLFRPEKCIAGTGLEGQAALDSGSVAIATQEGRIEYIDAVNITSSVNGDTVRTESVIYQRSNTNTCTHQKPQIHQGECVKKGQILADGATTVGGELSLGKNVLVAYMPWEGYNFEDAILISERLVYEDIYTSFHIVRYRIEICMTSQGPERITREIPHLDAHLLRHLDENGLVMLGSWIETGDVLVGKLTPQTIEESLCTPEGRLLQTIFGIEVSTARENCLRAPIGGRGRVIDVRWINRVDDSGDNAETVHVYISQKRKIQVGDKVSGRHGNKGIISIVLPRQDMPYLQNGIPVDMVLNPLGVPSRMNVGQIFECLPGLAGNPMNKHYRITPFDEKYEREASRKLVFPELYKASEQTANPWVFEPDHPGKHRLIDGRTGDVFEQPVTIGKAYMSKLSHQVDEKIHARSSGPYARVTQQPLRGKSKRGGQRIGEMEVWALEGFGVAYILQEMLTLKSDHIRTRNEVLGAIITGGPIPKPDTAPESFRLLIRELRSLALELNHAIISEKNFQIDREEV","length":1075,"molWeight":122471,"crc64":"00677BC6D8F26ACA","md5":"0F65B35EDEAEB1B34E4F81201E09207D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00001346EE"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41643","uniProtkbId":"PSBC_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":95,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Photosystem II CP43 reaction center protein"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"PSII 43 kDa protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Protein CP-43"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"psbC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"value":"Belongs to the PsbB/PsbC family. PsbC subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Propeptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"featureId":"PRO_0000431195"},{"type":"Chain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Photosystem II CP43 reaction center protein","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"featureId":"PRO_0000077525"},{"type":"Transmembrane","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Transmembrane","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Transmembrane","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Transmembrane","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Transmembrane","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Transmembrane","location":{"start":{"value":447,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Binding site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:189552"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}],"ligand":{"name":"[CaMn4O5] cluster","id":"ChEBI:CHEBI:189552"}},{"type":"Modified residue","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"N-acetylthreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]},{"type":"Modified residue","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01496"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04424.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07548","properties":[{"key":"EntryName","value":"T07548"}]},{"database":"RefSeq","id":"NP_042469.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41643","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41643","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809042","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016168","properties":[{"key":"GoTerm","value":"F:chlorophyll binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009772","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.10.10.670:FF:000001","properties":[{"key":"EntryName","value":"Photosystem II CP43 reaction center protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.670","properties":[{"key":"EntryName","value":"photosystem ii from thermosynechococcus elongatus"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01496","properties":[{"key":"EntryName","value":"PSII_PsbC_CP43"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000932","properties":[{"key":"EntryName","value":"PS_antenna-like"}]},{"database":"InterPro","id":"IPR036001","properties":[{"key":"EntryName","value":"PS_II_antenna-like_sf"}]},{"database":"InterPro","id":"IPR005869","properties":[{"key":"EntryName","value":"PSII_PsbC"}]},{"database":"InterPro","id":"IPR044900","properties":[{"key":"EntryName","value":"PSII_PsbC_sf"}]},{"database":"NCBIfam","id":"TIGR01153","properties":[{"key":"EntryName","value":"psbC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00421","properties":[{"key":"EntryName","value":"PSII"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161077","properties":[{"key":"EntryName","value":"Photosystem II antenna protein-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTLYSLRRSYPVETLFNGTIALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEIVDTFPYFVSGVLHLISSAVLGFGGIYHALIGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGVGAFLPVLKALYFGGVYDTWAPGGGDVRKITNPTLNPSAIFGYLLKSPFGGEGWIVSVDNLEDVIGGHVWLGSICIFGGIWHILTKPFAWARRAFVWSGEAYLSYSLAALSLFGFIACCFVWFNNTVYPSEFYGPTGPEASQAQAFTFLVRDQRLGASVGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDLRAPWLEPLRGPNGLDLSKLRKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN","length":473,"molWeight":51827,"crc64":"0E05E8FC7268465C","md5":"72F4759EAF576DE7998B72D82785503C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Propeptide":1,"Chain":1,"Transmembrane":6,"Binding site":1,"Modified residue":2},"uniParcId":"UPI0000132633"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41609","uniProtkbId":"CLPP_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":102,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"ATP-dependent Clp protease proteolytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"3.4.21.92"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Endopeptidase Clp"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"clpP"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).","ecNumber":"3.4.21.92","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}]}},{"texts":[{"value":"Component of the chloroplastic Clp protease core complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Plastid, chloroplast stroma","id":"SL-0055"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Belongs to the peptidase S14 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"ATP-dependent Clp protease proteolytic subunit","featureId":"PRO_0000179755"},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}]},{"type":"Active site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00444"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04336.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07458","properties":[{"key":"EntryName","value":"T07458"}]},{"database":"RefSeq","id":"NP_042379.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41609","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41609","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"S14.002","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809090","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.4.21.92","properties":[{"key":"OrganismId","value":"4862"}]},{"database":"GO","id":"GO:0009570","properties":[{"key":"GoTerm","value":"C:chloroplast stroma"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009368","properties":[{"key":"GoTerm","value":"C:endopeptidase Clp complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07017","properties":[{"key":"EntryName","value":"S14_ClpP_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000006","properties":[{"key":"EntryName","value":"ATP-dependent Clp protease proteolytic subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00444","properties":[{"key":"EntryName","value":"ClpP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001907","properties":[{"key":"EntryName","value":"ClpP"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR023562","properties":[{"key":"EntryName","value":"ClpP/TepA"}]},{"database":"InterPro","id":"IPR033135","properties":[{"key":"EntryName","value":"ClpP_His_AS"}]},{"database":"InterPro","id":"IPR018215","properties":[{"key":"EntryName","value":"ClpP_Ser_AS"}]},{"database":"PANTHER","id":"PTHR10381","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381:SF15","properties":[{"key":"EntryName","value":"CHLOROPLASTIC ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00574","properties":[{"key":"EntryName","value":"CLP_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00127","properties":[{"key":"EntryName","value":"CLPPROTEASEP"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00382","properties":[{"key":"EntryName","value":"CLP_PROTEASE_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00381","properties":[{"key":"EntryName","value":"CLP_PROTEASE_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPVGVPKVPFRAPGDEDATWVDLYNRLYRERLLFLAQDINHEIANQLMGLMVYLSAEDSNKDIFSFINCPGGSVIPGVGLFDMMQAIVPDVHTICMGVAASMGSFILIGGEMPKRIALPHARIMIHQPASSYYDGSAADFHNESKHVTMLRDYITRCYIERTDQPGEVIQRDLNRDVFMSATEAQAYGIVDVVAEG","length":196,"molWeight":21771,"crc64":"A10320956D89B0E1","md5":"8FB8976EA35C3F23FCAB6962690C3F4B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2},"uniParcId":"UPI0000127B4F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41627","uniProtkbId":"PSBH_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":92,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Photosystem II reaction center protein H"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"PSII-H"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Photosystem II 10 kDa phosphoprotein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"psbH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Phosphorylation is a light-dependent reaction catalyzed by a membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the N-terminus of the protein"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}],"value":"Belongs to the PsbH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56780"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"Photosystem II reaction center protein H","featureId":"PRO_0000070529"},{"type":"Transmembrane","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}]},{"type":"Modified residue","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":3,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}]},{"type":"Modified residue","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00752"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04389.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07511","properties":[{"key":"EntryName","value":"T07511"}]},{"database":"RefSeq","id":"NP_042432.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41627","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41627","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809009","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042301","properties":[{"key":"GoTerm","value":"F:phosphate ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015979","properties":[{"key":"GoTerm","value":"P:photosynthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050821","properties":[{"key":"GoTerm","value":"P:protein stabilization"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.5.880","properties":[{"key":"EntryName","value":"Photosystem II reaction center protein H"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00752","properties":[{"key":"EntryName","value":"PSII_PsbH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001056","properties":[{"key":"EntryName","value":"PSII_PsbH"}]},{"database":"InterPro","id":"IPR036863","properties":[{"key":"EntryName","value":"PSII_PsbH_sf"}]},{"database":"NCBIfam","id":"NF002728","properties":[{"key":"EntryName","value":"psbH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34469","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II REACTION CENTER PROTEIN H"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34469:SF4","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II REACTION CENTER PROTEIN H"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00737","properties":[{"key":"EntryName","value":"PsbH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161025","properties":[{"key":"EntryName","value":"Photosystem II 10 kDa phosphoprotein PsbH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATQTIDDTSKTTPKETLVGTTLKPLNSEYGKVAPGWGTTPLMGFAMALFAVFLSIILEIYNSSVLLDGIPVSWG","length":75,"molWeight":8007,"crc64":"78373947CF97FA9D","md5":"1255FCECB7ACD2BB84D1B3C140C79508"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Transmembrane":1,"Modified residue":2},"uniParcId":"UPI000016389D"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P10049","uniProtkbId":"CB21_PINTH","entryAudit":{"firstPublicDate":"1989-07-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1989-07-01","entryVersion":106,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"value":"Chlorophyll a-b binding protein type I, chloroplastic"},"shortNames":[{"value":"CAB"},{"value":"LHCP"}]},"flag":"Precursor"},"comments":[{"texts":[{"value":"The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin."}]}},{"texts":[{"value":"The LHC complex consists of chlorophyll a-b binding proteins"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"value":"The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Photoregulated by reversible phosphorylation of its threonine residues"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Chloroplast","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Chain","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Chlorophyll a-b binding protein type I, chloroplastic","featureId":"PRO_0000003692"},{"type":"Transmembrane","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"1"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"1"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"1"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"2"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"2"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"3"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"2"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"3"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"4"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P07371"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"5"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"4"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"2"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"5"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"3"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"4"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"1"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"5"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12333"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"6"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"6"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61721"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"chlorophyll b","id":"ChEBI:CHEBI:61721","label":"5"}},{"type":"Modified residue","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"N2-acetylarginine","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Modified residue","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0603","category":"Cellular component","name":"Photosystem I"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0809","category":"Domain","name":"Transit peptide"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"3062585","citationType":"journal article","authors":["Yamamoto N.","Matsuoka M.","Kano-Murakami Y.","Tanaka Y.","Ohashi Y."],"citationCrossReferences":[{"database":"PubMed","id":"3062585"},{"database":"DOI","id":"10.1093/nar/16.24.11829"}],"title":"Nucleotide sequence of a full length cDNA clone of light harvesting chlorophyll a/b binding protein gene from green dark-grown pine (Pinus tunbergii) seedling.","publicationDate":"1988","journal":"Nucleic Acids Res.","firstPage":"11829","lastPage":"11829","volume":"16"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X13407","properties":[{"key":"ProteinId","value":"CAA31773.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"PIR","id":"S02045","properties":[{"key":"EntryName","value":"S02045"}]},{"database":"AlphaFoldDB","id":"P10049","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P10049","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009765","properties":[{"key":"GoTerm","value":"P:photosynthesis, light harvesting"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.10.3460.10:FF:000001","properties":[{"key":"EntryName","value":"Chlorophyll a-b binding protein, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3460.10","properties":[{"key":"EntryName","value":"Chlorophyll a/b binding protein domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001344","properties":[{"key":"EntryName","value":"Chloro_AB-bd_pln"}]},{"database":"InterPro","id":"IPR022796","properties":[{"key":"EntryName","value":"Chloroa_b-bind"}]},{"database":"PANTHER","id":"PTHR21649","properties":[{"key":"EntryName","value":"CHLOROPHYLL A/B BINDING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00504","properties":[{"key":"EntryName","value":"Chloroa_b-bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103511","properties":[{"key":"EntryName","value":"Chlorophyll a-b binding protein"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATASAIQSSSLAGQTLLRPQQNELVKKVGTAQARITMRRTVRSAPESIWYGPDRPKYLGPFSEGTPSYLTGEFPGDYGWDTAAVSADPETFAKNRELEVIHCRWAMLGALGCVFPELLAKNGLKFGEAVWFKAGAQIFSEGGLDYAGNPNLIHAQSILAIWACQVVLMGLIEGYRVGGGTLGEGLDPLLPGGAFDPLGLADDPEACAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPIENLYDHLADPVANNAWAYATNFVPGK","length":266,"molWeight":28544,"crc64":"DFB592FC60420659","md5":"4D4CFFB2FF705E076050C37616D97883"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Transit peptide":1,"Chain":1,"Transmembrane":4,"Binding site":22,"Modified residue":2},"uniParcId":"UPI0000127117"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41616","uniProtkbId":"PSBF_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1995-11-01","entryVersion":100,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"Cytochrome b559 subunit beta"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"PSII reaction center subunit VI"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"psbF"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"value":"Belongs to the PsbE/PsbF family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"Cytochrome b559 subunit beta","featureId":"PRO_0000200441"},{"type":"Transmembrane","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}]},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00643"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413","note":"ligand shared with alpha subunit"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04354.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07476","properties":[{"key":"EntryName","value":"T07476"}]},{"database":"RefSeq","id":"NP_042397.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41616","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41616","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"808993","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009539","properties":[{"key":"GoTerm","value":"C:photosystem II reaction center"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009767","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport chain"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"HAMAP","id":"MF_00643","properties":[{"key":"EntryName","value":"PSII_PsbF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006217","properties":[{"key":"EntryName","value":"PSII_cyt_b559_asu"}]},{"database":"InterPro","id":"IPR006241","properties":[{"key":"EntryName","value":"PSII_cyt_b559_bsu"}]},{"database":"InterPro","id":"IPR006216","properties":[{"key":"EntryName","value":"PSII_cyt_b559_CS"}]},{"database":"InterPro","id":"IPR013081","properties":[{"key":"EntryName","value":"PSII_cyt_b559_N"}]},{"database":"NCBIfam","id":"TIGR01333","properties":[{"key":"EntryName","value":"cyt_b559_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33391:SF9","properties":[{"key":"EntryName","value":"CYTOCHROME B559 SUBUNIT BETA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00283","properties":[{"key":"EntryName","value":"Cytochrom_B559"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000037","properties":[{"key":"EntryName","value":"PsbF"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161045","properties":[{"key":"EntryName","value":"Cytochrome b559 subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00537","properties":[{"key":"EntryName","value":"CYTOCHROME_B559"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIDRTYPIFTVRWLAVHGLAIPTVFFLGSISAMQFIQR","length":39,"molWeight":4498,"crc64":"F6043D552D6E1C6F","md5":"BE904C63A4EF7DDE83B9B188930A7D53"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":1,"Binding site":1},"uniParcId":"UPI00000017C3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41644","uniProtkbId":"PSBD_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":122,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Photosystem II D2 protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"PSII D2 protein"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"1.10.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Photosystem Q(A) protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"psbD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 a plastoquinone + 4 hnu + 2 H2O = 2 a plastoquinol + O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36359"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:30212"},{"database":"ChEBI","id":"CHEBI:62192"}],"ecNumber":"1.10.3.9","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"value":"Belongs to the reaction center PufL/M/PsbA/D family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56761"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Photosystem II D2 protein","featureId":"PRO_0000090517"},{"type":"Transmembrane","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]},{"type":"Transmembrane","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]},{"type":"Transmembrane","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]},{"type":"Transmembrane","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]},{"type":"Transmembrane","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}]},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"ChlzD2"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:136840"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"pheophytin a","id":"ChEBI:CHEBI:136840","label":"D2"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:136840"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"pheophytin a","id":"ChEBI:CHEBI:136840","label":"D2"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58416"},{"database":"ChEBI","id":"CHEBI:25107"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"chlorophyll a","id":"ChEBI:CHEBI:58416","label":"PD2"},"ligandPart":{"name":"Mg","id":"ChEBI:CHEBI:25107"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17757"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"a plastoquinone","id":"ChEBI:CHEBI:17757","label":"Q(A)"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17757"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"a plastoquinone","id":"ChEBI:CHEBI:17757","label":"Q(A)"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01383"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"ligand shared with heterodimeric partner"}},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylthreonine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56761"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P56761"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0148","category":"Ligand","name":"Chlorophyll"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0604","category":"Cellular component","name":"Photosystem II"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04425.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07549","properties":[{"key":"EntryName","value":"T07549"}]},{"database":"RefSeq","id":"NP_042470.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41644","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41644","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809003","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009523","properties":[{"key":"GoTerm","value":"C:photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016168","properties":[{"key":"GoTerm","value":"F:chlorophyll binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010242","properties":[{"key":"GoTerm","value":"F:oxygen evolving activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009772","properties":[{"key":"GoTerm","value":"P:photosynthetic electron transport in photosystem II"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd09288","properties":[{"key":"EntryName","value":"Photosystem-II_D2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.85.10:FF:000001","properties":[{"key":"EntryName","value":"photosystem II D2 protein-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.85.10","properties":[{"key":"EntryName","value":"Photosystem II protein D1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01383","properties":[{"key":"EntryName","value":"PSII_PsbD_D2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR055266","properties":[{"key":"EntryName","value":"D1/D2"}]},{"database":"InterPro","id":"IPR036854","properties":[{"key":"EntryName","value":"Photo_II_D1/D2_sf"}]},{"database":"InterPro","id":"IPR000484","properties":[{"key":"EntryName","value":"Photo_RC_L/M"}]},{"database":"InterPro","id":"IPR055265","properties":[{"key":"EntryName","value":"Photo_RC_L/M_CS"}]},{"database":"InterPro","id":"IPR005868","properties":[{"key":"EntryName","value":"PSII_PsbD/D2"}]},{"database":"NCBIfam","id":"TIGR01152","properties":[{"key":"EntryName","value":"psbD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149:SF12","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II D2 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33149","properties":[{"key":"EntryName","value":"PHOTOSYSTEM II PROTEIN D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00124","properties":[{"key":"EntryName","value":"Photo_RC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00256","properties":[{"key":"EntryName","value":"REACTNCENTRE"}]},{"database":"SUPFAM","id":"SSF81483","properties":[{"key":"EntryName","value":"Bacterial photosystem II reaction centre, L and M subunits"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00244","properties":[{"key":"EntryName","value":"REACTION_CENTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIALGKSSKEEKTLFDTVDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDLTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPESETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL","length":353,"molWeight":39365,"crc64":"07151023CE35A325","md5":"DF5B9B967762E831F18546785B25FFB5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Transmembrane":5,"Binding site":8,"Modified residue":2},"uniParcId":"UPI000013264C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41645","uniProtkbId":"CHLL_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":120,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"DPOR subunit L"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"LI-POR subunit L"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"chlL"},"synonyms":[{"value":"frxC"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Binds 1 [4Fe-4S] cluster per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"value":"Belongs to the NifH/BchL/ChlL family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein","featureId":"PRO_0000139566"},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00355"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04440.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07564","properties":[{"key":"EntryName","value":"T07564"}]},{"database":"RefSeq","id":"NP_042485.2","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41645","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41645","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"808990","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02032","properties":[{"key":"EntryName","value":"Bchl-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00355","properties":[{"key":"EntryName","value":"ChlL_BchL"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR030655","properties":[{"key":"EntryName","value":"NifH/chlL_CS"}]},{"database":"InterPro","id":"IPR000392","properties":[{"key":"EntryName","value":"NifH/frxC"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005971","properties":[{"key":"EntryName","value":"Protochlorophyllide_ATP-bd"}]},{"database":"NCBIfam","id":"TIGR01281","properties":[{"key":"EntryName","value":"DPOR_bchL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42864","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42864:SF2","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00142","properties":[{"key":"EntryName","value":"Fer4_NifH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000363","properties":[{"key":"EntryName","value":"Nitrogenase_iron"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00091","properties":[{"key":"EntryName","value":"NITROGNASEII"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00746","properties":[{"key":"EntryName","value":"NIFH_FRXC_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00692","properties":[{"key":"EntryName","value":"NIFH_FRXC_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51026","properties":[{"key":"EntryName","value":"NIFH_FRXC_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSRRDLINKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGFEPSLNYVCNYYLGIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKNNKENLLGFTRI","length":291,"molWeight":31788,"crc64":"9FC619ABBC3FBBA6","md5":"8A3057D07D53CFCF9A15BE8B773DD36C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":6},"uniParcId":"UPI0000127883"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P41646","uniProtkbId":"CHLN_PINTH","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":87,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Light-independent protochlorophyllide reductase subunit N"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"DPOR subunit N"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"LI-POR subunit N"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"1.3.7.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"chlN"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28202"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83348"},{"database":"ChEBI","id":"CHEBI:83350"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"1.3.7.7","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"value":"Belongs to the BchN/ChlN family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Light-independent protochlorophyllide reductase subunit N","featureId":"PRO_0000208620"},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00352"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"ligand shared with heterodimeric partner"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0149","category":"Biological process","name":"Chlorophyll biosynthesis"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04441.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07565","properties":[{"key":"EntryName","value":"T07565"}]},{"database":"RefSeq","id":"NP_042486.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P41646","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P41646","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809019","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00670","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016730","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on iron-sulfur proteins as donors"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016636","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036068","properties":[{"key":"GoTerm","value":"P:light-independent chlorophyll biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019685","properties":[{"key":"GoTerm","value":"P:photosynthesis, dark reaction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01979","properties":[{"key":"EntryName","value":"Pchlide_reductase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1980","properties":[{"key":"EntryName","value":"Nitrogenase molybdenum iron protein domain"},{"key":"MatchStatus","value":"3"}]},{"database":"HAMAP","id":"MF_00352","properties":[{"key":"EntryName","value":"ChlN_BchN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050293","properties":[{"key":"EntryName","value":"LIPOR_BchN/ChlN"}]},{"database":"InterPro","id":"IPR000510","properties":[{"key":"EntryName","value":"Nase/OxRdtase_comp1"}]},{"database":"InterPro","id":"IPR005970","properties":[{"key":"EntryName","value":"Protochl_reductN"}]},{"database":"NCBIfam","id":"TIGR01279","properties":[{"key":"EntryName","value":"DPOR_bchN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002768","properties":[{"key":"EntryName","value":"PRK02842.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39429","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39429:SF3","properties":[{"key":"EntryName","value":"LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00148","properties":[{"key":"EntryName","value":"Oxidored_nitro"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000162","properties":[{"key":"EntryName","value":"P_chlorophyll_rd"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53807","properties":[{"key":"EntryName","value":"Helical backbone' metal receptor"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTKIVETITLECETGNYHSFCPISCVSWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAHLNDYEELKTLCIRIRKDRDPSVIIWIGTCTTEIIKMDLEGMAPKLEYEIGVPILVARANGLDYAFTQGEDTVLAVMAHRCPDQELPIGESKETKTKLFPFPLLKEKNLVEYANHPPLVIFGSLPSNLVSQLDTELRRQFIKVSGWLPAQRYADLPSLGDGVYVCGVNPFLSRTATTLIRRKKCELIVAPFPIGPDGTRAWIERICPVFGIEAQSLEEREERIWESLKDYLDLVRGKSVFFMGDNLIEISIARFLIRCGMIVYEIGIPYMDKRYQAAELALLQNTCIRMCMPIPRIVEKPDNSNQIRRMRELQPDLAITGMAHANPLGARGIGTKWSVEFTFAQIHGFANARDVLELVTRPLRRNENLDNLDRTTLVRKNNELYTSTPVK","length":467,"molWeight":53012,"crc64":"EA96C7FF8568329C","md5":"862484798CB7EC16E2B5F5F6A5F1EAE3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":3},"uniParcId":"UPI0000127893"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P52733","uniProtkbId":"RPOC1_PINTH","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-10-01","entryVersion":102,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"DNA-directed RNA polymerase subunit beta'"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"PEP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"Plastid-encoded RNA polymerase subunit beta'"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"RNA polymerase subunit beta'"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"rpoC1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"Binds 1 Zn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"value":"Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase subunit beta'","featureId":"PRO_0000067891"},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":504,"modifier":"EXACT"},"end":{"value":504,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":506,"modifier":"EXACT"},"end":{"value":506,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01323"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA23472.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07447","properties":[{"key":"EntryName","value":"T07447"}]},{"database":"RefSeq","id":"NP_042368.1","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P52733","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P52733","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"809013","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.40.90","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.40.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.860.120","properties":[{"key":"EntryName","value":"RNA polymerase II, clamp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.274.100","properties":[{"key":"EntryName","value":"RNA polymerase Rpb1, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01323","properties":[{"key":"EntryName","value":"RNApol_bact_RpoC1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045867","properties":[{"key":"EntryName","value":"DNA-dir_RpoC_beta_prime"}]},{"database":"InterPro","id":"IPR000722","properties":[{"key":"EntryName","value":"RNA_pol_asu"}]},{"database":"InterPro","id":"IPR006592","properties":[{"key":"EntryName","value":"RNA_pol_N"}]},{"database":"InterPro","id":"IPR007080","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_1"}]},{"database":"InterPro","id":"IPR042102","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_3_sf"}]},{"database":"InterPro","id":"IPR044893","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_clamp_domain"}]},{"database":"InterPro","id":"IPR034678","properties":[{"key":"EntryName","value":"RNApol_RpoC1"}]},{"database":"PANTHER","id":"PTHR19376","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19376:SF54","properties":[{"key":"EntryName","value":"DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04997","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00623","properties":[{"key":"EntryName","value":"RNA_pol_Rpb1_2"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00663","properties":[{"key":"EntryName","value":"RPOLA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64484","properties":[{"key":"EntryName","value":"beta and beta-prime subunits of DNA dependent RNA-polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIDQNKHQQLRIGLASPEQICAWSEKILPNGEIVGQVTKPHTLHYETNKPERDGSFCERIFGPIKSGVCSCGNSPGIGNEKIDAKFCTQCGVEFVDSRIRRYQMGYIKLACPVVHVWYLKRLPSYIANLLAKTRKELEGPVYCDLFLARPIANKPTLLRSRGTFDYEIQSWREIIPHYLSARPYYLFPRGSGTFKEREIATGGDAIGKQLMGLDLQMIIDRSHMEWKNLVELKWNRLEENQESTVDRWEDEKIRRRKDFLVGRMKLAKHFLRTNIEPKWMVLCLLPVLPPEPRPIVQLGEGGLITSSDLNELYRRVINRNNTLTNLLARSGSESFVIYQTKLIQEAVDALLDNGICRQPMRDSHNRPYKSFSDVIEGKEGRFRENLLGKRVDYSGRSVIVVGPFLSLYQCGLPSEIAIELFQAFLIRSLIGRHIAPNLRTAKSMIRDKGPIVWEVLQEVMQGHPILLNRAPTLHKLGIQAFQPILVEGRAIRLHPSVCGGFNADFDGDQMAVHVPLSLEARAEARLLMFSETNLLSPAIGDPISIPTQDMLLGLYISTVQNSQGIYGNRYHPYHSENKSFSCKKPSFYSYDDVLRAYRQKRIDLYSPLWLRWGEVDLRIITSVNQEAPIEVQYESLGTFHEIHEHYRIRKGRMGEILNIYIRTTVGRTRFNREMEEAIQGFACSEHPNKSLPALRI","length":696,"molWeight":79805,"crc64":"722B50492E077A63","md5":"018838B5BA2720949DF750739CFB9DB3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":7},"uniParcId":"UPI0000134734"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P69400","secondaryAccessions":["P52805"],"uniProtkbId":"PETL_PINTH","entryAudit":{"firstPublicDate":"2005-03-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-05-02","entryVersion":63,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Pinus thunbergii","commonName":"Japanese black pine","synonyms":["Pinus thunbergiana"],"taxonId":3350,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Pinopsida","Pinidae","Conifers I","Pinales","Pinaceae","Pinus","Pinus subgen. Pinus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Cytochrome b6-f complex subunit 6"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Cytochrome b6-f complex subunit PetL"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Cytochrome b6-f complex subunit VI"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"petL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"commentType":"RNA EDITING","locationType":"Known","positions":[{"position":"1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8710946"}]},{"position":"27","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8710946"}]},{"position":"34","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8710946"}]}],"note":{"texts":[{"value":"The initiator methionine is created by RNA editing. The stop codon at position 34 is created by RNA editing"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}],"value":"Belongs to the PetL family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Cytochrome b6-f complex subunit 6","featureId":"PRO_0000220469"},{"type":"Transmembrane","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00433"}]}],"geneLocations":[{"geneEncodingType":"Chloroplast"}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0691","category":"Coding sequence diversity","name":"RNA editing"},{"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"7937893","citationType":"journal article","authors":["Wakasugi T.","Tsudzuki J.","Ito S.","Nakashima K.","Tsudzuki T.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"7937893"},{"database":"DOI","id":"10.1073/pnas.91.21.9794"}],"title":"Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii.","publicationDate":"1994","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9794","lastPage":"9798","volume":"91"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"8710946","citationType":"journal article","authors":["Wakasugi T.","Hirose T.","Horihata M.","Tsudzuki T.","Koessel H.","Sugiura M."],"citationCrossReferences":[{"database":"PubMed","id":"8710946"},{"database":"DOI","id":"10.1073/pnas.93.16.8766"}],"title":"Creation of a novel protein-coding region at the RNA level in black pine chloroplasts: the pattern of RNA editing in the gymnosperm chloroplast is different from that in angiosperms.","publicationDate":"1996","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"8766","lastPage":"8770","volume":"93"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","RNA EDITING"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D17510","properties":[{"key":"ProteinId","value":"BAA04348.1"},{"key":"Status","value":"ALT_SEQ"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T07470","properties":[{"key":"EntryName","value":"T07470"}]},{"database":"RefSeq","id":"NP_042391.2","properties":[{"key":"NucleotideSequenceId","value":"NC_001631.1"}]},{"database":"AlphaFoldDB","id":"P69400","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P69400","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009512","properties":[{"key":"GoTerm","value":"C:cytochrome b6f complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00433","properties":[{"key":"EntryName","value":"Cytb6_f_PetL"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR007802","properties":[{"key":"EntryName","value":"Cyt_b6/f_cplx_su6"}]},{"database":"PANTHER","id":"PTHR37266","properties":[{"key":"EntryName","value":"CYTOCHROME B6-F COMPLEX SUBUNIT 6"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR37266:SF1","properties":[{"key":"EntryName","value":"CYTOCHROME B6-F COMPLEX SUBUNIT 6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05115","properties":[{"key":"EntryName","value":"PetL"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPTITIISYFGFLLASIIFTLVLFISLSKIQLI","length":33,"molWeight":3718,"crc64":"85D28F4CFA9000F6","md5":"4116ACB54BE9FD555F079178DFC39EB0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"RNA EDITING":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":1},"uniParcId":"UPI00004B2696"}}]}