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Database: UniProt
Entry: G8ISG7_9SPER
LinkDB: G8ISG7_9SPER
Original site: G8ISG7_9SPER 
ID   G8ISG7_9SPER            Unreviewed;        81 AA.
AC   G8ISG7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Photosystem I iron-sulfur center {ECO:0000256|ARBA:ARBA00013413, ECO:0000256|HAMAP-Rule:MF_01303};
DE            EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197, ECO:0000256|HAMAP-Rule:MF_01303};
DE   AltName: Full=9 kDa polypeptide {ECO:0000256|ARBA:ARBA00032541, ECO:0000256|HAMAP-Rule:MF_01303};
DE   AltName: Full=PSI-C {ECO:0000256|ARBA:ARBA00033423, ECO:0000256|HAMAP-Rule:MF_01303};
DE   AltName: Full=Photosystem I subunit VII {ECO:0000256|ARBA:ARBA00030218, ECO:0000256|HAMAP-Rule:MF_01303};
DE   AltName: Full=PsaC {ECO:0000256|ARBA:ARBA00031003, ECO:0000256|HAMAP-Rule:MF_01303};
GN   Name=psaC {ECO:0000256|HAMAP-Rule:MF_01303,
GN   ECO:0000313|EMBL:AET45138.1};
GN   ORFNames=PCL_14670 {ECO:0000313|EMBL:AET45138.1};
OS   Pinus yecorensis.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AET45138.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=644370 {ECO:0000313|EMBL:AET45138.1};
RN   [1] {ECO:0000313|EMBL:AET45138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YECO02 {ECO:0000313|EMBL:AET45138.1};
RX   PubMed=22731878; DOI=10.1186/1471-2148-12-100;
RA   Parks M., Cronn R., Liston A.;
RT   "Separating the wheat from the chaff: mitigating the effects of noise in a
RT   plastome phylogenomic data set from Pinus L. (Pinaceae).";
RL   BMC Evol. Biol. 12:100-100(2012).
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       {ECO:0000256|ARBA:ARBA00003402, ECO:0000256|HAMAP-Rule:MF_01303}.
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         Evidence={ECO:0000256|ARBA:ARBA00000994, ECO:0000256|HAMAP-
CC         Rule:MF_01303};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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 is
CC       most probably FB. {ECO:0000256|HAMAP-Rule:MF_01303};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_01303}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01303}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000256|HAMAP-
CC       Rule:MF_01303}.
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DR   EMBL; JN854152; AET45138.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8ISG7; -.
DR   SMR; G8ISG7; -.
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   Gene3D; 3.30.70.20; -; 1.
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   NCBIfam; TIGR03048; PS_I_psaC; 1.
DR   PANTHER; PTHR24960:SF79; PHOTOSYSTEM I IRON-SULFUR CENTER; 1.
DR   PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01303};
KW   Chloroplast {ECO:0000313|EMBL:AET45138.1};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01303};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01303};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01303}; Membrane {ECO:0000256|HAMAP-Rule:MF_01303};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01303};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01303};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_01303};
KW   Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP-
KW   Rule:MF_01303}; Plastid {ECO:0000313|EMBL:AET45138.1};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01303};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01303};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01303}.
FT   DOMAIN          1..31
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          39..68
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01303"
SQ   SEQUENCE   81 AA;  9008 MW;  C907CB61F25603A9 CRC64;
     MAHSVKIYDT CIGCTQCVRA CPTDVLEMIP WEGCKAKQIA SAPRTEDCAG CKRCESACPT
     DFLSVRVYLW HETTRSMGLA Y
//
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