PSAC_VITVI
ID PSAC_VITVI Reviewed; 81 AA.
AC Q0ZIW7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Photosystem I iron-sulfur center {ECO:0000255|HAMAP-Rule:MF_01303};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_01303};
DE AltName: Full=9 kDa polypeptide {ECO:0000255|HAMAP-Rule:MF_01303};
DE AltName: Full=PSI-C {ECO:0000255|HAMAP-Rule:MF_01303};
DE AltName: Full=Photosystem I subunit VII {ECO:0000255|HAMAP-Rule:MF_01303};
DE AltName: Full=PsaC {ECO:0000255|HAMAP-Rule:MF_01303};
GN Name=psaC {ECO:0000255|HAMAP-Rule:MF_01303};
OS Vitis vinifera (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Maxxa;
RX PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA Daniell H.;
RT "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT genome sequences: effects of taxon sampling and phylogenetic methods on
RT resolving relationships among rosids.";
RL BMC Evol. Biol. 6:32-32(2006).
CC -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC photosystem I (PSI); essential for photochemical activity. FB is the
CC terminal electron acceptor of PSI, donating electrons to ferredoxin.
CC The C-terminus interacts with PsaA/B/D and helps assemble the protein
CC into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI
CC is a plastocyanin-ferredoxin oxidoreductase, converting photonic
CC excitation into a charge separation, which transfers an electron from
CC the donor P700 chlorophyll pair to the spectroscopically characterized
CC acceptors A0, A1, FX, FA and FB in turn. {ECO:0000255|HAMAP-
CC Rule:MF_01303}.
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_01303};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01303};
CC Note=Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the
CC spectroscopically characterized electron acceptor FA and cluster 1 is
CC most probably FB. {ECO:0000255|HAMAP-Rule:MF_01303};
CC -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC subunits. {ECO:0000255|HAMAP-Rule:MF_01303}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01303}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000255|HAMAP-
CC Rule:MF_01303}.
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DR EMBL; DQ424856; ABE47586.1; -; Genomic_DNA.
DR RefSeq; YP_002608376.1; NC_012119.1.
DR RefSeq; YP_567129.1; NC_007957.1.
DR AlphaFoldDB; Q0ZIW7; -.
DR SMR; Q0ZIW7; -.
DR STRING; 29760.VIT_00s0246g00200.t01; -.
DR GeneID; 4025040; -.
DR GeneID; 7498557; -.
DR KEGG; vvi:4025040; -.
DR KEGG; vvi:7498557; -.
DR eggNOG; ENOG502S26M; Eukaryota.
DR InParanoid; Q0ZIW7; -.
DR OrthoDB; 1535519at2759; -.
DR Proteomes; UP000009183; Chloroplast.
DR ExpressionAtlas; Q0ZIW7; baseline.
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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IBA:GO_Central.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:InterPro.
DR HAMAP; MF_01303; PSI_PsaC; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR017491; PSI_PsaC.
DR TIGRFAMs; TIGR03048; PS_I_psaC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Chloroplast; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I; Plastid;
KW Reference proteome; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000276005"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT DOMAIN 39..68
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
SQ SEQUENCE 81 AA; 9038 MW; 68071DB57FC603BF CRC64;
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
DFLSVRVYLW HETTRSMGLA Y
