PSAA_AMPOP
ID PSAA_AMPOP Reviewed; 671 AA.
AC Q9MTQ4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12;
DE AltName: Full=PSI-A;
DE AltName: Full=PsaA;
DE Flags: Fragment;
GN Name=psaA;
OS Amphidinium operculatum (Dinoflagellate).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC Amphidinium.
OX NCBI_TaxID=107036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCAP 1102/6;
RX PubMed=10732684; DOI=10.1007/s004380050042;
RA Barbrook A.C., Howe C.J.;
RT "Minicircular plastid DNA in the dinoflagellate Amphidinium operculatum.";
RL Mol. Gen. Genet. 263:152-158(2000).
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;
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:0000250};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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; AJ250264; CAB75844.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MTQ4; -.
DR SMR; Q9MTQ4; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1130.10; -; 2.
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; 3.
DR Pfam; PF00223; PsaA_PsaB; 3.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 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..671
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088530"
FT TRANSMEM 68..91
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..168
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..209
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..277
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..318
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..360
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..399
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..469
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..530
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..606
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 493
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 595
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:0000250"
FT BINDING 603
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:0000250"
FT BINDING 611
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 612
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 671 AA; 73320 MW; C5E7908E350C2A21 CRC64;
VYQERFDIVQ PHCSSEHTIS LNTDFSKAAF GSATGLVAKA ASQTTTAIWN LHADAHDFSN
SSYLSKQVFA ANLAHIGVVF IWLSGMHFHG AYFSNYLDWL QDPSIAPTAQ QVSNIANQSV
LNPIRVTSGF FNLWLAEGIT STYQLKVIAA FGLIASALCF LGSYFHMHSS TSFTRVLNTK
LTSLSTHHLV GLLGLGSLAW AGHLIHISLP VNILLNAGVA VPSPHSLLSS KAVATIVEQL
SFSALTSSDG YVWQPLVYSA MHHFALALVL IVGSVLGPLS TASNPLMSFT VGSSWHLVLG
VQLFVTGTAS VLYAQMSNAY PVYPYLLTDH PTVVSLFVHH MWIGGFFLVG AFAHLSIGLV
RDTLPQSFSV VLTQRDIILG HLTWVVAFLG VHSFGLYVHN DTMQALGRPD DMFSDNAISL
LPVFARWSTL TLNSTGSAVS VLGVELSTAD FMVTHIHAFT IHTTVLILVK GFLYARSSRL
VNDKYKLDFR YPCDGPGRGG TCQISPWDHV FLGLFWMYNS ISVVIFHFFW EYQSNLASIK
ASAGGSIRAL ASDFELNSIN TNGWLRNFLW SGAAQVIQSY GSPLAAYGLT FLASHFVWAL
SLMFLFSGRG YWQELIESVL WAHHKLYVVP HIQPRALSIT SGRAVGLTHY LLGGIGTTWS
FFLARIVATA G
