PSAC_SYNP2
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 03-AUG-2022, entry version 154.
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; Synechococcus;
OC unclassified 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 Publishers,
RL 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., Wang J.,
RA 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 assembly
RT of a [3Fe-4S] cluster in PsaC of photosystem I. The photoreduction of FA is
RT 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 constraints
RT for the formation of iron-sulfur clusters in free and 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 of a
RT mixed ligand [4Fe-4S] cluster in the C51D mutant of PsaC upon rebinding to
RT 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 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 -!- FUNCTION: Mutant proteins with a 3Fe-4S center are not observed bound
CC 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 [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;
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 is
CC most probably FB.;
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
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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 AlphaFoldDB; P31087; -.
DR SMR; P31087; -.
DR STRING; 32049.SYNPCC7002_A1589; -.
DR EnsemblBacteria; ACA99580; ACA99580; SYNPCC7002_A1589.
DR KEGG; syp:SYNPCC7002_A1589; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_139698_8_0_3; -.
DR OMA; GHMSHAV; -.
DR EvolutionaryTrace; P31087; -.
DR Proteomes; UP000001688; 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 DisProt; DP00935; -.
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; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Reference proteome; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1551590"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062021"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 37..68
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT MUTAGEN 14
FT /note="C->A,D,S: Generates altered FB cluster (in vitro)."
FT /evidence="ECO:0000269|PubMed:1318744,
FT ECO:0000269|PubMed:7499299"
FT MUTAGEN 21
FT /note="C->D: Unable to bind PSI cores (in vitro)."
FT /evidence="ECO:0000269|PubMed:7499299"
FT MUTAGEN 34
FT /note="C->A,S: No measurable effect."
FT /evidence="ECO:0000269|PubMed:7499299"
FT MUTAGEN 51
FT /note="C->A,D,S: Generates altered FA cluster (in vitro)."
FT /evidence="ECO:0000269|PubMed:1318744,
FT ECO:0000269|PubMed:7499299, ECO:0000269|PubMed:7499300"
FT MUTAGEN 58
FT /note="C->D: Unable to bind PSI cores (in vitro)."
FT /evidence="ECO:0000269|PubMed:7499299"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1K0T"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1K0T"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1K0T"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1K0T"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1K0T"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1K0T"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1K0T"
SQ SEQUENCE 81 AA; 8814 MW; 57B7D4A3371A4AFB CRC64;
MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG AETTRSMGLA Y
