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PSAC_GLOVI
ID   PSAC_GLOVI              Reviewed;          81 AA.
AC   Q7NG86;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
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}; OrderedLocusNames=gsl3287;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CHARACTERIZATION OF PHOTOSYSTEM I.
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=15589832; DOI=10.1016/j.febslet.2004.11.013;
RA   Inoue H., Tsuchiya T., Satoh S., Miyashita H., Kaneko T., Tabata S.,
RA   Tanaka A., Mimuro M.;
RT   "Unique constitution of photosystem I with a novel subunit in the
RT   cyanobacterium Gloeobacter violaceus PCC 7421.";
RL   FEBS Lett. 578:275-279(2004).
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   -!- 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 G.violaceus PSI reaction center is composed of one copy
CC       each of PsaA,B,C,D,E,F,L,M and Z, and forms trimeric complexes.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC       Cytoplasmic side.
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DR   EMBL; BA000045; BAC91228.1; -; Genomic_DNA.
DR   RefSeq; NP_926233.1; NC_005125.1.
DR   RefSeq; WP_011143277.1; NC_005125.1.
DR   PDB; 7F4V; EM; 2.04 A; aC/bC/cC=1-81.
DR   PDBsum; 7F4V; -.
DR   AlphaFoldDB; Q7NG86; -.
DR   SMR; Q7NG86; -.
DR   STRING; 251221.35213858; -.
DR   EnsemblBacteria; BAC91228; BAC91228; BAC91228.
DR   KEGG; gvi:gsl3287; -.
DR   PATRIC; fig|251221.4.peg.3319; -.
DR   eggNOG; COG1143; Bacteria.
DR   HOGENOM; CLU_139698_8_0_3; -.
DR   InParanoid; Q7NG86; -.
DR   OMA; GHMSHAV; -.
DR   OrthoDB; 1873445at2; -.
DR   PhylomeDB; Q7NG86; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:InterPro.
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   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem I; Reference proteome; Repeat;
KW   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_0000062011"
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;  8798 MW;  9CDA6A97234B0BF5 CRC64;
     MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGNKAGTIA SSPRTEDCVG CKRCETACPT
     DFLSIRVYLG AETTRSMGLA Y
 
 
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