ID A0A0G4KC33_9FLOR Unreviewed; 751 AA. AC A0A0G4KC33; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 03-AUG-2022, entry version 23. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000256|ARBA:ARBA00017774, ECO:0000256|HAMAP-Rule:MF_00458}; DE EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197, ECO:0000256|HAMAP-Rule:MF_00458}; DE AltName: Full=PsaA {ECO:0000256|ARBA:ARBA00031004, ECO:0000256|HAMAP-Rule:MF_00458}; GN Name=psaA {ECO:0000256|HAMAP-Rule:MF_00458, GN ECO:0000313|EMBL:CRF40148.1}; OS Laurencia snackeyi. OG Plastid {ECO:0000313|EMBL:CRF40148.1}. OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales; OC Rhodomelaceae; Laurencieae; Laurencia. OX NCBI_TaxID=1858662 {ECO:0000313|EMBL:CRF40148.1, ECO:0000313|Proteomes:UP000307987}; RN [1] {ECO:0000313|Proteomes:UP000307987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=28061748; DOI=10.1186/s12864-016-3453-0; RA Ng P.K., Lin S.M., Lim P.E., Liu L.C., Chen C.M., Pai T.W.; RT "Complete chloroplast genome of Gracilaria firma (Gracilariaceae, RT Rhodophyta), with discussion on the use of chloroplast phylogenomics in the RT subclass Rhodymeniophycidae."; RL BMC Genomics 18:40-40(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:49552; EC=1.97.1.12; CC Evidence={ECO:0000256|ARBA:ARBA00000994, ECO:0000256|HAMAP- CC Rule:MF_00458}; CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair CC and subsequent electron acceptors. PSI consists of a core antenna CC complex that captures photons, and an electron transfer chain that CC converts photonic excitation into a charge separation. The eukaryotic CC PSI reaction center is composed of at least 11 subunits. CC {ECO:0000256|ARBA:ARBA00026002}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00458}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. CC {ECO:0000256|ARBA:ARBA00010598, ECO:0000256|HAMAP-Rule:MF_00458}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LN833431; CRF40148.1; -; Genomic_DNA. DR Proteomes; UP000307987; Chromosome plastid. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.1130.10; -; 1. DR HAMAP; MF_00458; PSI_PsaA; 1. DR InterPro; IPR006243; PSI_PsaA. DR InterPro; IPR001280; PSI_PsaA/B. DR InterPro; IPR020586; PSI_PsaA/B_CS. DR InterPro; IPR036408; PSI_PsaA/B_sf. DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; SSF81558; 1. DR TIGRFAMs; TIGR01335; psaA; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00458}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00458}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00458}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP- KW Rule:MF_00458}; Plastid {ECO:0000313|EMBL:CRF40148.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00458}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00458}. FT TRANSMEM 73..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 159..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 353..373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 393..415 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 436..457 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 538..557 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 592..612 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 665..687 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 728..748 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 575 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 584 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 676 FT /ligand="chlorophyll a'" FT /ligand_id="ChEBI:CHEBI:189419" FT /ligand_label="A1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 684 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="A3" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 692 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="A3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 693 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="A" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" SQ SEQUENCE 751 AA; 83790 MW; 685A1C8CA89390E8 CRC64; MTTSSKEQET NKVKVSVDKN PVTTSFEKWA KPGHFSRTLA KGPNTTTWIW NLHADAHDFD SHTNSLEDIS RKIFSAHFGQ LAIIFLWLSG MYFHGARFSN YVAWLNNPTL IKPSAQVVWP IVGQEILNAD VGGGFQGVQI TSGFFQLWRS SGITTEFELY ATAIGGLFMS LLMVFAGWFH YHKSAPKLEW FQNVESMMNH HLAGLLGLGC LGWSGHQIHI ALPINKLLDS GVSPQEIPLP HEFIVNRSLM SELYPSFSKG ILPFFTLNWS EYSDFLTFKG GLNPINGGLW LSDIAHHHLA LSVMFLVAGH MYRTNWGIGH SMKEILEAHK GPFTGEGHKG LYEILTTSWH AQLAINLAMM GSLSIIVAHH MYAMPPYPYI ATDYATQLSL FTHHMWIGGF CVVGAGAHAS IFMVRDYNPA QNYDNVLDRV IRHRDAIISH LNWLCIFLGF HSFGLYIHND TMRALGRSQD MFSDTGIQLQ PIFAQWIQNI HTLAPSNTSP NSLATASYAF GGDTIAVANK IAMMPIKLGT ADFMVHHIHA FTIHVTVLIL VKGFLFARNS RLIPDKSNLG FRFPCDGPGR GGTCQVSAWD HVFLGLFWMY NSLSIVIFHF SWKMQSDVWG SIKGTEISHI AGGNFSQSAI TINGWLRDFL WAQASQVIQS YGSALSAYGL IFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKVKVA PSIQPRALSI TQGRAVGLAH YLLGGIGTTW AFFLARIISL G //