{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q57564","uniProtkbId":"ASST_METJA","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-11-01","entryVersion":110,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","commonName":"Methanococcus jannaschii","taxonId":243232,"lineage":["Archaea","Methanobacteriati","Methanobacteriota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}],"value":"L-aspartate semialdehyde sulfurtransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}],"value":"2.8.1.16"}]}},"genes":[{"orderedLocusNames":[{"value":"MJ0100"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}],"value":"Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0099, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. Likely functions through persulfide intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate 4-semialdehyde + reduced 2[4Fe-4S]-[ferredoxin] + hydrogen sulfide + 3 H(+) = oxidized 2[4Fe-4S]-[ferredoxin] + L-homocysteine + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58412"},{"database":"Rhea","id":"RHEA-COMP:10002"},{"database":"Rhea","id":"RHEA-COMP:10004"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29919"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33723"},{"database":"ChEBI","id":"CHEBI:58199"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"2.8.1.16","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"value":"The ligand-induced conformational reorganization of the protein could be an important regulatory mechanism"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}],"value":"Amino-acid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18931440"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"value":"Homodimer (PubMed:18931440, PubMed:20026078). May form a complex with MJ0099 (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"value":"The C-terminal cystathionine beta-synthase (CBS) domains can bind different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5'-thioadenosine (MTA) ligands. Binding of SAM and MTA triggers a drastic conformational change in the protein, which evolves progressively from an open form in the absence of ligands to a closed form when the four sites are fully occupied"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the L-aspartate semialdehyde sulfurtransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"L-aspartate semialdehyde sulfurtransferase","featureId":"PRO_0000106693"},{"type":"Domain","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"CBS 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00703"}]},{"type":"Domain","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"CBS 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00703"}]},{"type":"Active site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TPT4"}]},{"type":"Binding site","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20026078"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Helix","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPD"}]},{"type":"Helix","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Helix","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Helix","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Helix","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Beta strand","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]},{"type":"Helix","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3KPB"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"id":"KW-0129","category":"Domain","name":"CBS domain"},{"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0677","category":"Domain","name":"Repeat"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"8688087","citationType":"journal article","authors":["Bult C.J.","White O.","Olsen G.J.","Zhou L.","Fleischmann R.D.","Sutton G.G.","Blake J.A.","FitzGerald L.M.","Clayton R.A.","Gocayne J.D.","Kerlavage A.R.","Dougherty B.A.","Tomb J.-F.","Adams M.D.","Reich C.I.","Overbeek R.","Kirkness E.F.","Weinstock K.G.","Merrick J.M.","Glodek A.","Scott J.L.","Geoghagen N.S.M.","Weidman J.F.","Fuhrmann J.L.","Nguyen D.","Utterback T.R.","Kelley J.M.","Peterson J.D.","Sadow P.W.","Hanna M.C.","Cotton M.D.","Roberts K.M.","Hurst M.A.","Kaine B.P.","Borodovsky M.","Klenk H.-P.","Fraser C.M.","Smith H.O.","Woese C.R.","Venter J.C."],"citationCrossReferences":[{"database":"PubMed","id":"8688087"},{"database":"DOI","id":"10.1126/science.273.5278.1058"}],"title":"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.","publicationDate":"1996","journal":"Science","firstPage":"1058","lastPage":"1073","volume":"273"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"18931440","citationType":"journal article","authors":["Lucas M.","Kortazar D.","Astigarraga E.","Fernandez J.A.","Mato J.M.","Martinez-Chantar M.L.","Martinez-Cruz L.A."],"citationCrossReferences":[{"database":"PubMed","id":"18931440"},{"database":"DOI","id":"10.1107/s1744309108027930"}],"title":"Purification, crystallization and preliminary X-ray diffraction analysis of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100.","publicationDate":"2008","journal":"Acta Crystallogr. F","firstPage":"936","lastPage":"941","volume":"64"},"referencePositions":["CRYSTALLIZATION","SUBUNIT"]},{"referenceNumber":3,"citation":{"id":"20026078","citationType":"journal article","authors":["Lucas M.","Encinar J.A.","Arribas E.A.","Oyenarte I.","Garcia I.G.","Kortazar D.","Fernandez J.A.","Mato J.M.","Martinez-Chantar M.L.","Martinez-Cruz L.A."],"citationCrossReferences":[{"database":"PubMed","id":"20026078"},{"database":"DOI","id":"10.1016/j.jmb.2009.12.012"}],"title":"Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair.","publicationDate":"2010","journal":"J. Mol. Biol.","firstPage":"800","lastPage":"820","volume":"396"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 388-509 IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND S-METHYL-5'-THIOADENOSINE","ACTIVITY REGULATION","SUBUNIT","DOMAIN"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"3KPB"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3KPC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"3KPD"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L77117","properties":[{"key":"ProteinId","value":"AAB98080.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"D64312","properties":[{"key":"EntryName","value":"D64312"}]},{"database":"PDB","id":"3KPB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B/C/D=388-509"}]},{"database":"PDB","id":"3KPC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.79 A"},{"key":"Chains","value":"A=386-509"}]},{"database":"PDB","id":"3KPD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.91 A"},{"key":"Chains","value":"A/B/C/D=388-509"}]},{"database":"PDBsum","id":"3KPB","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"3KPC","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"3KPD","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"Q57564","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q57564","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"Q57564","properties":[{"key":"Number of interactors","value":"20"}]},{"database":"STRING","id":"243232.MJ_0100","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"243232-MJ_0100","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAB98080","properties":[{"key":"ProteinId","value":"AAB98080"},{"key":"GeneId","value":"MJ_0100"}]},{"database":"KEGG","id":"mja:MJ_0100","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"arCOG00620","properties":[{"key":"ToxonomicScope","value":"Archaea"}]},{"database":"HOGENOM","id":"CLU_043239_0_0_2","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"Q57564","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"295172at2157","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"Q57564","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.8.1.16","properties":[{"key":"OrganismId","value":"3260"}]},{"database":"EvolutionaryTrace","id":"Q57564","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000805","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"CDD","id":"cd04605","properties":[{"key":"EntryName","value":"CBS_pair_arch_MET2_assoc"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.580.10","properties":[{"key":"EntryName","value":"CBS-domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000644","properties":[{"key":"EntryName","value":"CBS_dom"}]},{"database":"InterPro","id":"IPR046342","properties":[{"key":"EntryName","value":"CBS_dom_sf"}]},{"database":"InterPro","id":"IPR051257","properties":[{"key":"EntryName","value":"Diverse_CBS-Domain"}]},{"database":"InterPro","id":"IPR002708","properties":[{"key":"EntryName","value":"HcyBio"}]},{"database":"InterPro","id":"IPR016426","properties":[{"key":"EntryName","value":"MA1821-like"}]},{"database":"PANTHER","id":"PTHR43080:SF2","properties":[{"key":"EntryName","value":"CBS DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43080","properties":[{"key":"EntryName","value":"CBS DOMAIN-CONTAINING PROTEIN CBSX3, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00571","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF01837","properties":[{"key":"EntryName","value":"HcyBio"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF004698","properties":[{"key":"EntryName","value":"UCP004698_CBS_MJ0100"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00116","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54631","properties":[{"key":"EntryName","value":"CBS-domain pair"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51371","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MIMKTIKEINEKIKKGEAVVVTAEEMIKIVEEEGAKRAADYVDVVTTGTFGAMCSSGVFINFGHSDPPIKMLRIYLNNVEAYGGLAAVDAYIGAAQPNEDPDVDIDYGGAHVIEDLVRGKEVELYAEGYTTDCYPRKEVNVRITLDDVNQAIMVNPRNCYQTYAAATNSREEKIYTYMGILLPEYNNVHYSGAGQLNPLQNDYNPETKSFNTIGIGTRIFLGGGIGYVIGEGTQHNPPFGTLMVKGDLKQMNPKFIRAATMPRYGSTLYVGIGIPIPVLNEKIAERCAIRDEDIEVPIYDYGFPRRDRPLIAKTNYKVLRSGKITLNVNIDGKDVEKTVKTGSVSSYKMAREVAETLKQWILDGKFLLTERVDTLGRAENKPMKSPITLVKDILSKPPITAHSNISIMEAAKILIKHNINHLPIVDEHGKLVGIITSWDIAKALAQNKKTIEEIMTRNVITAHEDEPVDHVAIKMSKYNISGVPVVDDYRRVVGIVTSEDISRLFGGKK","length":509,"molWeight":56458,"crc64":"81417970CD74F38F","md5":"613DA4F2D7B89DD63EA0FEC8861CCB36"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Active site":1,"Binding site":8,"Helix":6,"Beta strand":6},"uniParcId":"UPI0000139270"}}