ID   A0A088CJW0_9VIRI        Unreviewed;       751 AA.
AC   A0A088CJW0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 29.
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}.
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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   PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1.
DR   PANTHER; PTHR30128:SF75; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2; 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   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}; 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|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
//