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Database: UniProt
Entry: Q119B1
LinkDB: Q119B1
Original site: Q119B1 
ID   PSAC_TRIEI              Reviewed;          81 AA.
AC   Q119B1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 85.
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=Tery_0454;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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
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 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:0000255|HAMAP-Rule:MF_01303}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01303}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01303}; Cytoplasmic side
CC       {ECO:0000255|HAMAP-Rule:MF_01303}.
DR   EMBL; CP000393; ABG49913.1; -; Genomic_DNA.
DR   RefSeq; WP_006616272.1; NC_008312.1.
DR   ProteinModelPortal; Q119B1; -.
DR   SMR; Q119B1; -.
DR   STRING; 203124.Tery_0454; -.
DR   PRIDE; Q119B1; -.
DR   EnsemblBacteria; ABG49913; ABG49913; Tery_0454.
DR   KEGG; ter:Tery_0454; -.
DR   eggNOG; ENOG4108Z6M; Bacteria.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000230505; -.
DR   KO; K02691; -.
DR   OMA; AHTVKIY; -.
DR   OrthoDB; 1873445at2; -.
DR   BioCyc; TERY203124:G1G6S-472-MONOMER; -.
DR   Proteomes; UP000008878; 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   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem I; Reference proteome; Repeat; Thylakoid; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2     81       Photosystem I iron-sulfur center.
FT                                /FTId=PRO_0000292108.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01303}.
FT   DOMAIN       37     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;  8814 MW;  52633F33371A4AFB CRC64;
     MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA SSPRTEDCIG CKRCETACPT
     DFLSVRVYLG AETTRSMGLA Y
//
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