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Database: UniProt
Entry: P31085
LinkDB: P31085
Original site: P31085 
ID   PSAC_SYNP6              Reviewed;          81 AA.
AC   P31085;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 128.
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=syc0986_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
OS   (Anacystis nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8016272; DOI=10.1104/pp.104.4.1459;
RA   Herman P.L., Adiwilaga K., Golbeck J.H., Weeks D.P.;
RT   "Sequence of a psaC gene from the cyanobacterium Synechococcus sp. PCC
RT   6301.";
RL   Plant Physiol. 104:1459-1461(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular
RT   cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene
RT   content and organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-19.
RX   PubMed=1653017; DOI=10.1016/S0005-2728(05)80206-3;
RA   Li N., Warren P.V., Golbeck J.H., Frank G., Zuber H., Bryant D.A.;
RT   "Polypeptide composition of the Photosystem I complex and the
RT   Photosystem I core protein from Synechococcus sp. PCC 6301.";
RL   Biochim. Biophys. Acta 1059:215-225(1991).
RN   [4]
RP   MUTAGENESIS OF ASP-9; GLU-27 AND ASP-32.
RX   PubMed=8794765; DOI=10.1021/bi9612834;
RA   Rodday S.M., Do L.T., Chynwat V., Frank H.A., Biggins J.;
RT   "Site-directed mutagenesis of the subunit PsaC establishes a surface-
RT   exposed domain interacting with the photosystem I core binding site.";
RL   Biochemistry 35:11832-11838(1996).
RN   [5]
RP   FUNCTION.
RX   PubMed=9545061; DOI=10.1016/S0006-3495(98)77909-3;
RA   Vassiliev I.R., Jung Y.-S., Yang F., Golbeck J.H.;
RT   "PsaC subunit of photosystem I is oriented with iron-sulfur cluster
RT   F(B) as the immediate electron donor to ferredoxin and flavodoxin.";
RL   Biophys. J. 74:2029-2035(1998).
RN   [6]
RP   MUTAGENESIS OF THE C-TERMINUS.
RX   PubMed=8621546; DOI=10.1074/jbc.271.15.8996;
RA   Naver H., Scott M.P., Golbeck J.H., Moeller B.L., Scheller H.V.;
RT   "Reconstitution of barley photosystem I with modified PSI-C allows
RT   identification of domains interacting with PSI-D and PSI-A/B.";
RL   J. Biol. Chem. 271:8996-9001(1996).
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:0000269|PubMed:9545061}.
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.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
DR   EMBL; U01536; AAA18220.1; -; Unassigned_DNA.
DR   EMBL; AP008231; BAD79176.1; -; Genomic_DNA.
DR   RefSeq; WP_011243298.1; NC_006576.1.
DR   ProteinModelPortal; P31085; -.
DR   SMR; P31085; -.
DR   STRING; 269084.syc0986_d; -.
DR   EnsemblBacteria; BAD79176; BAD79176; syc0986_d.
DR   KEGG; syc:syc0986_d; -.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000230505; -.
DR   KO; K02691; -.
DR   OMA; AHTVKIY; -.
DR   BioCyc; SELO269084:G1G2F-1070-MONOMER; -.
DR   Proteomes; UP000001175; 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   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:1653017}.
FT   CHAIN         2     81       Photosystem I iron-sulfur center.
FT                                /FTId=PRO_0000062022.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       39     68       4Fe-4S ferredoxin-type 2.
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        21     21       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        51     51       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   MUTAGEN       9      9       D->A: Decreases assembly onto PSI cores
FT                                (in vitro). {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN       9      9       D->R: Decreases assembly onto PSI cores
FT                                in vitro, FA and FB seems to assemble
FT                                normally. {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN      27     27       E->A: No effect.
FT                                {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN      27     27       E->R: Decreases assembly onto PSI cores
FT                                in vitro, FA and FB seem to assemble
FT                                normally. {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN      32     32       D->A: No effect.
FT                                {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN      32     32       D->R: Decreases assembly onto PSI cores
FT                                in vitro, FA and FB seems to assemble
FT                                normally. {ECO:0000269|PubMed:8794765}.
FT   MUTAGEN      72     81       Missing: Required for stable assembly of
FT                                the protein onto PSI cores (in vitro).
FT                                {ECO:0000269|PubMed:8621546}.
SQ   SEQUENCE   81 AA;  8798 MW;  40010FD9371A4AFB CRC64;
     MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA ASPRTEDCVG CKRCETACPT
     DFLSIRVYLG AETTRSMGLA Y
//
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