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PSAA_OLTVI
ID   PSAA_OLTVI              Reviewed;         751 AA.
AC   Q20EW6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=PSI-A {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};
OS   Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC   Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX   NCBI_TaxID=51324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA   Pombert J.-F., Lemieux C., Turmel M.;
RT   "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT   viridis reveals a distinctive quadripartite architecture in the chloroplast
RT   genome of early diverging ulvophytes.";
RL   BMC Biol. 4:3-3(2006).
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.
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=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more
CC       chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-
CC       4S iron-sulfur center. {ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00458}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00458}.
CC   -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00458}.
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DR   EMBL; DQ291132; ABB81947.1; -; Genomic_DNA.
DR   RefSeq; YP_635879.1; NC_008099.1.
DR   AlphaFoldDB; Q20EW6; -.
DR   SMR; Q20EW6; -.
DR   GeneID; 4100126; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron;
KW   Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW   Photosynthesis; Photosystem I; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..751
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000275954"
FT   TRANSMEM        73..96
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        159..182
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        198..222
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        294..312
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        349..372
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        388..414
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        436..458
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        533..551
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        591..612
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        665..687
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        725..745
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         692
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="A3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         693
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ   SEQUENCE   751 AA;  83115 MW;  944512387ABA6B0F CRC64;
     MTISPPEREA KKVKIVVDRN PVETSLEKWA KPGHFSRALS KGPTTTTWIW NLHADAHDFD
     SHTSDLEDIS RKVFSAHFGQ LGIIFIWLSG MYFHGARFSN YEAWLSDPTH IKPSAQVVWP
     VVGQEILNGD VGGGFQGIQI TSGFFQLWRA SGITSELQLY ATAIGGLVMA AAMFFAGWFH
     YHKAAPKLEW FQNVESMMNH HLAGLLGLGS LAWAGHQIHI SLPINKLLDA GVDPKEIPLP
     HELMLNRELM AQLYPSFAKG LAPFFTLNWG EYSDFLTFQG GLNPVTGGLW LSDEAHHHLA
     IAVLFLIAGH QYRTNWGIGH SMKEILEAHK GPFTGEGHKG LYEILTTSWH AQLAINLAML
     GSLSIIVAHH MYAMPPYPYL ATDYGTQLSL FTHHVWIGGF CIVGAGAHAA IFMVRDYDPT
     NNYNNLLDRV IRHRDAIISH LNWVCIFLGF HSFGLYIHND TMSALGRPQD MFSDTAIQLQ
     PVFAQWVQNT HFLAPQLTAP NALAATSVSW GGDVVAVGGK VAMMPIALGT SDFLVHHIHA
     FTIHVTVLIL LKGVLYSRSS RLIPDKANLG FRFPCDGPGR GGTCQVSAWD HVFLGLFWMY
     NSLSIVIFHF SWKMQSDVWG SVTASGVTHI TGGNFAASAN TINGWLRDFL WAQSSQVIQS
     YGSALSAYGL MFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PAIQPRALSI
     TQGRAVGVAH YLLGGIATTW SFFLARIISV G
 
 
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