PSAC_SYNS9
ID PSAC_SYNS9 Reviewed; 81 AA.
AC Q3B0I2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=Syncc9902_0171;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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/cytochrome c6-ferredoxin oxidoreductase, converting
CC photonic excitation into a charge separation, which transfers an
CC electron from the donor P700 chlorophyll pair to the spectroscopically
CC characterized acceptors A0, A1, FX, FA and FB in turn.
CC {ECO:0000255|HAMAP-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 cyanobacterial PSI reaction center is composed of one copy
CC each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000255|HAMAP-Rule:MF_01303}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01303}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01303}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01303}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB25146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000097; ABB25146.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006850103.1; NC_007513.1.
DR AlphaFoldDB; Q3B0I2; -.
DR SMR; Q3B0I2; -.
DR STRING; 316279.Syncc9902_0171; -.
DR EnsemblBacteria; ABB25146; ABB25146; Syncc9902_0171.
DR KEGG; sye:Syncc9902_0171; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_139698_8_0_3; -.
DR OrthoDB; 1873445at2; -.
DR Proteomes; UP000002712; Chromosome.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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: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 Pfam; PF12838; Fer4_7; 1.
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; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Reference proteome; Repeat;
KW 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_0000292133"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT DOMAIN 37..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; 8842 MW; 49A83112370C8621 CRC64;
MSHAVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG DETTRSMGLA Y
