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Database: UniProt
Entry: P56301
LinkDB: P56301
Original site: P56301 
ID   PSAC_CHLVU              Reviewed;          81 AA.
AC   P56301;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-DEC-2018, entry version 95.
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   Chlorella vulgaris (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales;
OC   Chlorellaceae; Chlorella.
OX   NCBI_TaxID=3077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM C-27 / Tamiya;
RX   PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA   Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S.,
RA   Tsudzuki J., Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T.,
RA   Inamura A., Yoshinaga K., Sugiura M.;
RT   "Complete nucleotide sequence of the chloroplast genome from the green
RT   alga Chlorella vulgaris: the existence of genes possibly involved in
RT   chloroplast division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
CC   -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC       photosystem I (PSI); essential for photochemical activity. FB is
CC       the terminal electron acceptor of PSI, donating electrons to
CC       ferredoxin. The C-terminus interacts with PsaA/B/D and helps
CC       assemble the protein into the PSI complex. Required for binding of
CC       PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-
CC       ferredoxin oxidoreductase, converting photonic excitation into a
CC       charge separation, which transfers an electron from the donor P700
CC       chlorophyll pair to the spectroscopically characterized acceptors
CC       A0, A1, FX, FA and FB in turn. {ECO:0000255|HAMAP-Rule:MF_01303}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced
CC         [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-
CC         COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:49552;
CC         EC=1.97.1.12; Evidence={ECO:0000255|HAMAP-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
CC       is most probably FB. {ECO:0000255|HAMAP-Rule:MF_01303};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at
CC       least 11 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
CC       {ECO:0000255|HAMAP-Rule:MF_01303}.
DR   EMBL; AB001684; BAA57846.1; -; Genomic_DNA.
DR   PIR; T07199; T07199.
DR   RefSeq; NP_045771.1; NC_001865.1.
DR   ProteinModelPortal; P56301; -.
DR   SMR; P56301; -.
DR   GeneID; 809124; -.
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: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; Chloroplast; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I; Plastid;
KW   Repeat; Thylakoid; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2     81       Photosystem I iron-sulfur center.
FT                                /FTId=PRO_0000061975.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   DOMAIN       39     68       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        21     21       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        51     51       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
SQ   SEQUENCE   81 AA;  8818 MW;  C20250462755CA3D CRC64;
     MSHTVKIYDT CIGCTQCVRA CPTDVLEMVP WDGCKASQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLG SETTRSMGLA Y
//
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