ID PSAA_PROM5 Reviewed; 760 AA. AC A2BYP9; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000255|HAMAP-Rule:MF_00458}; DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00458}; DE AltName: Full=PsaA {ECO:0000255|HAMAP-Rule:MF_00458}; GN Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458}; GN OrderedLocusNames=P9515_17031; OS Prochlorococcus marinus (strain MIT 9515). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167542; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9515; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). 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:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00458}; CC -!- COFACTOR: CC Note=PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl CC chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core CC antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and CC 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a' CC dimer, A0 is one or more divinyl chlorophyll a, A1 is one or both CC phylloquinones and FX is a shared 4Fe-4S iron-sulfur center. CC {ECO:0000255|HAMAP-Rule:MF_00458}; CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 divinyl chlorophyll CC special pair and subsequent electron acceptors. PSI consists of a core CC antenna complex that captures photons, and an electron transfer chain CC that converts photonic excitation into a charge separation. The CC cyanobacterial PSI reaction center is composed of one copy each of CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes. CC {ECO:0000255|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP- CC Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00458}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP- CC 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; CP000552; ABM72910.1; -; Genomic_DNA. DR RefSeq; WP_011821002.1; NC_008817.1. DR AlphaFoldDB; A2BYP9; -. DR SMR; A2BYP9; -. DR STRING; 167542.P9515_17031; -. DR GeneID; 60200996; -. DR KEGG; pmc:P9515_17031; -. DR eggNOG; COG2885; Bacteria. DR HOGENOM; CLU_016126_1_0_3; -. DR OrthoDB; 499313at2; -. DR Proteomes; UP000001589; Chromosome. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell. 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; Chlorophyll; Chromophore; Electron transport; Iron; Iron-sulfur; KW Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis; KW Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..760 FT /note="Photosystem I P700 chlorophyll a apoprotein A1" FT /id="PRO_0000294203" FT TRANSMEM 76..99 FT /note="Helical; Name=I" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 162..185 FT /note="Helical; Name=II" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 201..225 FT /note="Helical; Name=III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 309..327 FT /note="Helical; Name=IV" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 368..391 FT /note="Helical; Name=V" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 407..433 FT /note="Helical; Name=VI" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 455..477 FT /note="Helical; Name=VII" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 551..569 FT /note="Helical; Name=VIII" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 609..630 FT /note="Helical; Name=IX" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 674..696 FT /note="Helical; Name=X" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 734..754 FT /note="Helical; Name=XI" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 593 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 602 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 685 FT /ligand="divinylchlorophyll a'" FT /ligand_id="ChEBI:CHEBI:189420" FT /ligand_label="A1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 693 FT /ligand="divinyl chlorophyll a" FT /ligand_id="ChEBI:CHEBI:73095" FT /ligand_label="A3" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 701 FT /ligand="divinyl chlorophyll a" FT /ligand_id="ChEBI:CHEBI:73095" FT /ligand_label="A3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 702 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="A" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" SQ SEQUENCE 760 AA; 83716 MW; E73A0882B41063EC CRC64; MTISPPESGE KDKKILESPV KADPRPIDFA KLDKPGFWSS KLSKGPKTTT WIWNLHADAH DFDVHTGDAE EATRKIFSAH FGHLAVIFIW MSAAFFHGAR FSNYSGWLAD PTHVKPGAQQ VWAIVGQEML NGDLGANYNG IQISSGVFHM WRAWGITNES ELMALAIGAV VMAALMLHAG IFHYHKAAPK MEWFQDVESM MNHHLAGLLG LGSLAWAGHT IHIGAPTAAL LDAIDAGSPL IINGKEIATI ADIPMPHQLC DPQIVGQIFP GLASGTGNFF SLNWFAFSDF LTFKGGLNPV TGSLWMTDIA HHHLAIAVLF IIAGHMYRTN YGIGHSMKEI LDAHQGDPIL FPAPRGHQGL FDFMAESRHA QLSVNLALLG SLSIIISHHM YAMPPYPYIA TDYMTVLGLF THHMWIGGLF IVGAGAHAGI AMVRDYDPAK HIDNVLDRVL KARDALISHL NWVCMWLGFH SFGLYIHNDT MRALGRPQDM FSDKAIQLQP IFAQWIQNIQ SSGVGTTLLE GNGVSQVFNG ETISVGGKVA MTGIPLGTAD LMIHHIHAFQ IHVTVLILLK GVLYARSSRL IPDKASLGFR FPCDGPGRGG TCQVSSWDHV FLALFWMYNC LSIVIFHFSW KMQSDVWGLT GGNFAQSAIT INGWLRDFLW AQAAQVLTSY GQSISMYGLM FLGAHFIWAF SLMFLFSGRG YWQELFESIV WAHNKLKVAP TIQPRALSIT QGRAVGVTHF LVGGIATTWA FFHARLFGIG //