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Database: UniProt
Entry: P31087
LinkDB: P31087
Original site: P31087 
ID   PSAC_SYNP2              Reviewed;          81 AA.
AC   P31087; B1XNQ5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-APR-2019, entry version 133.
DE   RecName: Full=Photosystem I iron-sulfur center;
DE            EC=1.97.1.12;
DE   AltName: Full=9 kDa polypeptide;
DE   AltName: Full=PSI-C;
DE   AltName: Full=Photosystem I subunit VII;
DE   AltName: Full=PsaC;
GN   Name=psaC; OrderedLocusNames=SYNPCC7002_A1589;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bryant D.A., Rhiel E., de Lorimier R., Zhou J., Stirewalt V.L.,
RA   Gasparich G.E., Dubbs J.M., Snyder W.;
RL   (In) Baltscheffsky M. (eds.);
RL   Current research in photosynthesis, pp.2:1-9, Kluwer Academic
RL   Publishers, Dordrecht (1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RX   PubMed=1551590; DOI=10.1016/0378-1119(92)90313-E;
RA   Rhiel E., Stirewalt V.L., Gasparich G.E., Bryant D.A.;
RT   "The psaC genes of Synechococcus sp. PCC7002 and Cyanophora paradoxa:
RT   cloning and sequence analysis.";
RL   Gene 112:123-128(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA   Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   MUTAGENESIS OF CYS-14 AND CYS-51.
RX   PubMed=1318744; DOI=10.1021/bi00137a001;
RA   Zhao J., Li N., Warren P.V., Golbeck J.H., Bryant D.A.;
RT   "Site-directed conversion of a cysteine to aspartate leads to the
RT   assembly of a [3Fe-4S] cluster in PsaC of photosystem I. The
RT   photoreduction of FA is independent of FB.";
RL   Biochemistry 31:5093-5099(1992).
RN   [5]
RP   MUTAGENESIS OF CYS-14; CYS-21; CYS-34; CYS-51 AND CYS-58.
RX   PubMed=7499299; DOI=10.1074/jbc.270.47.28108;
RA   Mehari T., Qiao F., Scott M.P., Nellis D.F., Zhao J., Bryant D.A.,
RA   Golbeck J.H.;
RT   "Modified ligands to FA and FB in photosystem I. I. Structural
RT   constraints for the formation of iron-sulfur clusters in free and
RT   rebound PsaC.";
RL   J. Biol. Chem. 270:28108-28117(1995).
RN   [6]
RP   MUTAGENESIS OF CYS-51.
RX   PubMed=7499300; DOI=10.1074/jbc.270.47.28118;
RA   Yu L., Vassiliev I.R., Jung Y.-S., Bryant D.A., Golbeck J.H.;
RT   "Modified ligands to FA and FB in photosystem I. II. Characterization
RT   of a mixed ligand [4Fe-4S] cluster in the C51D mutant of PsaC upon
RT   rebinding to P700-FX cores.";
RL   J. Biol. Chem. 270:28118-28125(1995).
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.
CC   -!- FUNCTION: Mutant proteins with a 3Fe-4S center are not observed
CC       bound to PSI in vitro, and are probably not able to do so in vivo.
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;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
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.;
CC   -!- SUBUNIT: The cyanobacterial PSI reaction center is composed of one
CC       copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric
CC       complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
DR   EMBL; M86238; AAA27353.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99580.1; -; Genomic_DNA.
DR   RefSeq; WP_012307203.1; NC_010475.1.
DR   PDB; 1K0T; NMR; -; A=2-81.
DR   PDBsum; 1K0T; -.
DR   DisProt; DP00935; -.
DR   ProteinModelPortal; P31087; -.
DR   SMR; P31087; -.
DR   STRING; 32049.SYNPCC7002_A1589; -.
DR   PRIDE; P31087; -.
DR   EnsemblBacteria; ACA99580; ACA99580; SYNPCC7002_A1589.
DR   KEGG; syp:SYNPCC7002_A1589; -.
DR   eggNOG; ENOG4108Z6M; Bacteria.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000230505; -.
DR   KO; K02691; -.
DR   OMA; AHTVKIY; -.
DR   EvolutionaryTrace; P31087; -.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C: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   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem I; Repeat; Thylakoid;
KW   Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1551590}.
FT   CHAIN         2     81       Photosystem I iron-sulfur center.
FT                                /FTId=PRO_0000062021.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       37     68       4Fe-4S ferredoxin-type 2.
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S).
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S).
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S).
FT   METAL        21     21       Iron-sulfur 2 (4Fe-4S).
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S).
FT   METAL        51     51       Iron-sulfur 2 (4Fe-4S).
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S).
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S).
FT   MUTAGEN      14     14       C->A,D,S: Generates altered FB cluster
FT                                (in vitro). {ECO:0000269|PubMed:1318744,
FT                                ECO:0000269|PubMed:7499299}.
FT   MUTAGEN      21     21       C->D: Unable to bind PSI cores (in
FT                                vitro). {ECO:0000269|PubMed:7499299}.
FT   MUTAGEN      34     34       C->A,S: No measurable effect.
FT                                {ECO:0000269|PubMed:7499299}.
FT   MUTAGEN      51     51       C->A,D,S: Generates altered FA cluster
FT                                (in vitro). {ECO:0000269|PubMed:1318744,
FT                                ECO:0000269|PubMed:7499299,
FT                                ECO:0000269|PubMed:7499300}.
FT   MUTAGEN      58     58       C->D: Unable to bind PSI cores (in
FT                                vitro). {ECO:0000269|PubMed:7499299}.
FT   STRAND       18     20       {ECO:0000244|PDB:1K0T}.
FT   STRAND       26     30       {ECO:0000244|PDB:1K0T}.
FT   STRAND       32     34       {ECO:0000244|PDB:1K0T}.
FT   STRAND       37     41       {ECO:0000244|PDB:1K0T}.
FT   STRAND       60     63       {ECO:0000244|PDB:1K0T}.
FT   TURN         69     71       {ECO:0000244|PDB:1K0T}.
FT   STRAND       74     79       {ECO:0000244|PDB:1K0T}.
SQ   SEQUENCE   81 AA;  8814 MW;  57B7D4A3371A4AFB CRC64;
     MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA SSPRTEDCVG CKRCETACPT
     DFLSIRVYLG AETTRSMGLA Y
//
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