位置:首页 > 蛋白库 > PSAC_WHEAT
PSAC_WHEAT
ID   PSAC_WHEAT              Reviewed;          81 AA.
AC   P69415; P10794;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
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   Triticum aestivum (Wheat).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND92000055; DOI=10.1007/BF00027388;
RA   Dunn P.P.J., Gray J.C.;
RT   "Localization and nucleotide sequence of the gene for the 8 kDa subunit of
RT   photosystem I in pea and wheat chloroplast DNA.";
RL   Plant Mol. Biol. 11:311-319(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA   Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA   Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT   "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT   sequence and contig clones.";
RL   Plant Mol. Biol. Rep. 18:243-253(2000).
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. {ECO:0000255|HAMAP-
CC       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; Evidence={ECO:0000255|HAMAP-
CC         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 is
CC       most probably FB. {ECO:0000255|HAMAP-Rule:MF_01303};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC       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 {ECO:0000255|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; X13158; CAA31555.1; -; Genomic_DNA.
DR   EMBL; AB042240; BAB47086.1; -; Genomic_DNA.
DR   PIR; S04034; FEWT1.
DR   RefSeq; NP_114309.1; NC_002762.1.
DR   AlphaFoldDB; P69415; -.
DR   SMR; P69415; -.
DR   STRING; 4565.EPlTAEP00000010009; -.
DR   PRIDE; P69415; -.
DR   EnsemblPlants; TraesCSU02G270000.1; TraesCSU02G270000.1.cds1; TraesCSU02G270000.
DR   GeneID; 803185; -.
DR   Gramene; TraesCSU02G270000.1; TraesCSU02G270000.1.cds1; TraesCSU02G270000.
DR   KEGG; taes:803185; -.
DR   eggNOG; ENOG502S26M; Eukaryota.
DR   HOGENOM; CLU_139698_8_0_1; -.
DR   OMA; KVDLWHE; -.
DR   Proteomes; UP000019116; Chloroplast.
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:0015979; P:photosynthesis; IBA:GO_Central.
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   Reference proteome; Repeat; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..81
FT                   /note="Photosystem I iron-sulfur center"
FT                   /id="PRO_0000062007"
FT   DOMAIN          2..31
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT   DOMAIN          39..68
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01303"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01303"
SQ   SEQUENCE   81 AA;  8899 MW;  681F63DC8FC603BF CRC64;
     MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLG PETTRSMALS Y
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024