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Database: UniProt
Entry: P62091
LinkDB: P62091
Original site: P62091 
ID   PSAC_ATRBE              Reviewed;          81 AA.
AC   P62091; P07136; P25252; Q9MRU0; Q9T2J4;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-DEC-2018, entry version 67.
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   Atropa belladonna (Belladonna) (Deadly nightshade).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Hyoscyameae; Atropa.
OX   NCBI_TaxID=33113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ab5p(kan);
RX   PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA   Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA   Maier R.M.;
RT   "The plastid chromosome of Atropa belladonna and its comparison with
RT   that of Nicotiana tabacum: the role of RNA editing in generating
RT   divergence in the process of plant speciation.";
RL   Mol. Biol. Evol. 19:1602-1612(2002).
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-ferredoxin
CC       oxidoreductase, converting photonic excitation into a charge
CC       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; AJ316582; CAC88097.1; -; Genomic_DNA.
DR   RefSeq; NP_783283.1; NC_004561.1.
DR   ProteinModelPortal; P62091; -.
DR   SMR; P62091; -.
DR   GeneID; 806469; -.
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   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_0000061971.
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;  9038 MW;  68071DB57FC603BF CRC64;
     MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLW HETTRSMGLA Y
//
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