ID A0A088CJW0_9VIRI Unreviewed; 751 AA. AC A0A088CJW0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 27-MAR-2024, entry version 31. 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=PSI-A {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:AID67522.1}; OS Prasinoderma coloniale. OG Plastid; Chloroplast {ECO:0000313|EMBL:AID67522.1}. OC Eukaryota; Viridiplantae; Prasinodermophyta; Prasinodermophyceae; OC Prasinodermales; Prasinodermaceae; Prasinoderma. OX NCBI_TaxID=156133 {ECO:0000313|EMBL:AID67522.1}; RN [1] {ECO:0000313|EMBL:AID67522.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25281016; DOI=10.1186/1471-2164-15-857; RA Lemieux C., Otis C., Turmel M.; RT "Six newly sequenced chloroplast genomes from prasinophyte green algae RT provide insights into the relationships among prasinophyte lineages and the RT diversity of streamlined genome architecture in picoplanktonic species."; RL BMC Genomics 15:857-857(2014). CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, CC converting photonic excitation into a charge separation, which CC transfers an electron from the donor P700 chlorophyll pair to the CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid CC membrane by plastocyanin or cytochrome c6. {ECO:0000256|HAMAP- CC Rule:MF_00458}. 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, ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00458}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00458}. 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; KJ746598; AID67522.1; -; Genomic_DNA. DR RefSeq; YP_009057464.1; NC_024817.1. DR AlphaFoldDB; A0A088CJW0; -. DR GeneID; 20357977; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. 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; Photosystem I PsaA/PsaB; 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 NCBIfam; TIGR01335; psaA; 1. DR PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1. DR PANTHER; PTHR30128:SF77; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; Photosystem I subunits PsaA/PsaB; 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}; Chloroplast {ECO:0000313|EMBL:AID67522.1}; 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:AID67522.1}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, 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 294..312 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 533..551 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 665..687 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; 83389 MW; EB0E2C5852646CD6 CRC64; MTIRPPKHEA KKIKILVDTN TVSTSFEKWA KPGHFSRTLA KGPTTTTWVW NLHADAHDFD SHTTDLEDIS RKVFSAHFGQ LGIILIWLSG MYFHGARFSN YEAWLTDPTN IKPSAQVVWP IVGQEILNGD VGGGFQGIQI TSGFFQLWRA SGITTELELY STAIGGLVLA GLMFFAGWFH YHKAAPKLEW FQSVESMMNH HLAGLLGLGS LAWAGHQIHV ALPINLLLDA GIDPKEIPLP HEFLLDRQLM AQLYPSFAQG LTPFFTMHWA AYGDFLTFKG GLNPVTGALW LTDIAHHHLA VAVLFIIAGH MYRTNWGIGH SFKEILEAHR GPFTGNGHKG LYEILTTSWH AQLAINLALF GSLSIIVAHH MYAMPAYPYI AVDYGTQLSL FTHHTWIGGF CICGAAAHGA IFMVRDYDPL NNYNNVLDRV IRHRDAIISH LNWVCIFLGF HSFGLYIHND TMSALGRPQD MFSDTALQLQ PVFAQWVQQT HMSAPDLTAP NALLGTSPAW GGDTIAINGK VAMMPVPLGT ADFMVHHIHA FTIHVTVLIL LKGVLFARSS RLIPDKANLG FRFPCDGPGR GGTCQVSGWD HVFLGLFWMY NCISVDIFYF SWKMQSDVWG TVTDQGISHI TGGNFALTAN TINGWLRDFL WAQSSQVLQA YGSALSAYSL TFLAAHFIWA FSLMFLFSGR GYWQELIESI VWAHNKLRVA PAIQPRALSI TQGRAVGVAH YLLGGICTTW AFFLARICAV G //