GenomeNet

Database: UniProt
Entry: E3T2P3_9TRAC
LinkDB: E3T2P3_9TRAC
Original site: E3T2P3_9TRAC 
ID   E3T2P3_9TRAC            Unreviewed;        81 AA.
AC   E3T2P3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:ADE18112.1};
OS   Isoetes flaccida.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADE18112.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Isoetales; Isoetaceae; Isoetes.
OX   NCBI_TaxID=49763 {ECO:0000313|EMBL:ADE18112.1};
RN   [1] {ECO:0000313|EMBL:ADE18112.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20969798; DOI=10.1186/1471-2148-10-321;
RA   Karol K.G., Arumuganathan K., Boore J.L., Duffy A.M., Everett K.D.,
RA   Hall J.D., Hansen S.K., Kuehl J.V., Mandoli D.F., Mishler B.D.,
RA   Olmstead R.G., Renzaglia K.S., Wolf P.G.;
RT   "Complete plastome sequences of Equisetum arvense and Isoetes flaccida:
RT   implications for phylogeny and plastid genome evolution of early land plant
RT   lineages.";
RL   BMC Evol. Biol. 10:321-321(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU191333; ADE18112.1; -; Genomic_DNA.
DR   RefSeq; YP_004021286.1; NC_014675.1.
DR   AlphaFoldDB; E3T2P3; -.
DR   GeneID; 9978054; -.
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; 1.
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:ADE18112.1};
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:ADE18112.1};
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;  8755 MW;  CD0C2E35D61ABEF4 CRC64;
     MAHSVKIYDT CIGCTQCVRA CLTDVSETVP WDGCKANQIA PAPRTEDCVG CKRCESACPT
     DFLSVRVYLG SETTRSTGLA Y
//
DBGET integrated database retrieval system