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PSAC_CUCSA
ID   PSAC_CUCSA              Reviewed;          81 AA.
AC   P42046; A5J1Y4; Q2QD40; Q4VZL7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Photosystem I iron-sulfur center;
DE            EC=1.97.1.12;
DE   AltName: Full=9 kDa polypeptide;
DE   AltName: Full=PS 1 subunit 11;
DE   AltName: Full=PSI-C;
DE   AltName: Full=Photosystem I subunit VII;
DE   AltName: Full=PsaC;
GN   Name=psaC; Synonyms=frxA; OrderedLocusNames=CsCp106;
OS   Cucumis sativus (Cucumber).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekmibaekdadagi;
RX   PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA   Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA   Choi D.-W., Liu J.R., Cho K.Y.;
RT   "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT   Baekmibaekdadagi) chloroplast genome.";
RL   Plant Cell Rep. 25:334-340(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Borszczagowski;
RX   PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA   Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT   "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT   genome: its composition and comparative analysis.";
RL   Cell. Mol. Biol. Lett. 12:584-594(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chipper, and cv. Gy14;
RX   PubMed=17546086; DOI=10.1139/g07-003;
RA   Chung S.-M., Gordon V.S., Staub J.E.;
RT   "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT   differences between chilling-tolerant and -susceptible cucumber lines.";
RL   Genome 50:215-225(2007).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-26.
RC   TISSUE=Cotyledon;
RX   PubMed=1883835; DOI=10.1016/s0005-2728(05)80198-7;
RA   Iwasaki Y., Ishikawa H., Hibino T., Takabe T.;
RT   "Characterization of genes that encode subunits of cucumber PS I complex by
RT   N-terminal sequencing.";
RL   Biochim. Biophys. Acta 1059:141-148(1991).
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-ferredoxin oxidoreductase, converting photonic
CC       excitation into a charge separation, which transfers an electron from
CC       the donor P700 chlorophyll pair to the spectroscopically characterized
CC       acceptors A0, A1, FX, FA and FB in turn.
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; Evidence={ECO:0000250};
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. {ECO:0000250};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC       {ECO:0000250}.
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DR   EMBL; DQ119058; AAZ94699.1; -; Genomic_DNA.
DR   EMBL; AJ970307; CAJ00810.1; -; Genomic_DNA.
DR   EMBL; DQ865975; ABI97464.1; -; Genomic_DNA.
DR   EMBL; DQ865976; ABI98795.1; -; Genomic_DNA.
DR   RefSeq; YP_247651.1; NC_007144.1.
DR   AlphaFoldDB; P42046; -.
DR   SMR; P42046; -.
DR   STRING; 3659.XP_004174172.1; -.
DR   GeneID; 3429272; -.
DR   KEGG; csv:3429272; -.
DR   eggNOG; ENOG502S26M; Eukaryota.
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   1: Evidence at protein level;
KW   4Fe-4S; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem I; Plastid; Repeat; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1883835"
FT   CHAIN           2..81
FT                   /note="Photosystem I iron-sulfur center"
FT                   /id="PRO_0000061976"
FT   DOMAIN          2..31
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          39..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                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   81 AA;  8980 MW;  680556D8CB5603BF CRC64;
     MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WGGCKAKQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLW HETTRSMGLA Y
 
 
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