PSAA_HETTR
ID PSAA_HETTR Reviewed; 732 AA.
AC Q9XQV3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Heterocapsa triquetra (Dinoflagellate) (Glenodinium triquetrum).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Peridiniales; Heterocapsaceae;
OC Heterocapsa.
OX NCBI_TaxID=66468;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCMP449;
RX PubMed=10408440; DOI=10.1038/22099;
RA Zhang Z., Green B.R., Cavalier-Smith T.;
RT "Single gene circles in dinoflagellate chloroplast genomes.";
RL Nature 400:155-159(1999).
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; AF130031; AAD44698.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XQV3; -.
DR SMR; Q9XQV3; -.
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; 2.
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..732
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088553"
FT TRANSMEM 61..84
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 145..168
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 185..209
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 278..296
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 317..340
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 356..382
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 414..436
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 510..528
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 568..589
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 644..666
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 704..724
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 552
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 561
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 655
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 663
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 671
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 672
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 732 AA; 80332 MW; 69AB9493629AF4C3 CRC64;
MKLFFRYVNS RVWSQAGSSH FNKALAKGPK TTTWIWSLHA DAHDFQQSSS ESTAASVGAK
VFSSGLAHFS IVFFWLGGMH FHGAYFSNYS AWLKDPKTPG SQLVWSLVGQ DILNQDLGGY
FQSIRVTSGF FQLWRAEGIV TQVHLKYAAA AALIGSIATL WAAYFHMHIS WSSSLRTMGS
LSSYNAGQLA ILAGLGSISW AGHQIHIALP INRLLDSGVD PSQLPSPQDL LFKDLMQVIF
PGFGVGPAVD FSIYLNQKGA ASEVGLNPST GSIYLGQIAS HHFFVGITCI ISGIIALLVK
RSKAGSFQDA AAFNNSWHSR LSINLAIAGS LSITFAHHIY AMPVYPFCGS DYATVLSLFV
HHMWIGGFFI VGAGAHASIF MIRDEGVPAG IPSAKGRLYS VNSIIQQLLA HRDIIMGHLI
YVTIALGMHA FGIYIHNDTL QALGRPEDIF SDNSIQLKPL FAVWVQSLPS LFLLNTLSGD
AAVTGIPGFG LEVLDGKVVT MTQELGTADF MVHHIHAFTI HCTLLILMKG VLYSRSSRLV
SDKLELGFRY PCDGPGRGGT CQISPWDHVF LGVFWMYNSL SIVIFHFFWK MQSDVWGVYD
VSTQKIVHLT GGDFSVNSIT INGWLRNFLW SQAAEVIQSY GSGLSGYGLI FLGAHFTWAF
SLMFLWSGRG YWQELIESIL WAHHKLKIVP NIQPRALSIT QGRAVGLVHY MLGGIGTTWA
FFLARVVALS IS
