FER_WHEAT
ID FER_WHEAT Reviewed; 143 AA.
AC P00228;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ferredoxin, chloroplastic;
DE Flags: Precursor;
GN Name=PETF;
OS Triticum aestivum (Wheat).
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].
RC STRAIN=cv. Chinese Spring;
RA Bringloe D.H., Gray J.C.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 47-143.
RX PubMed=486088; DOI=10.1042/bj1790373;
RA Takruri I.A.H., Boulter D.;
RT "The amino acid sequence of ferredoxin from Triticum aestivum (wheat).";
RL Biochem. J. 179:373-378(1979).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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; X75089; CAA52980.1; -; Genomic_DNA.
DR PIR; S52993; FEWT.
DR AlphaFoldDB; P00228; -.
DR SMR; P00228; -.
DR STRING; 4565.Traes_7BL_0B5D2BAF0.1; -.
DR PRIDE; P00228; -.
DR EnsemblPlants; TraesCAD_scaffold_002919_01G000100.1; TraesCAD_scaffold_002919_01G000100.1; TraesCAD_scaffold_002919_01G000100.
DR EnsemblPlants; TraesCAD_scaffold_134402_01G000100.1; TraesCAD_scaffold_134402_01G000100.1; TraesCAD_scaffold_134402_01G000100.
DR EnsemblPlants; TraesCAD_scaffold_166582_01G000100.1; TraesCAD_scaffold_166582_01G000100.1; TraesCAD_scaffold_166582_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_001556_01G000100.1; TraesCLE_scaffold_001556_01G000100.1; TraesCLE_scaffold_001556_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_165303_01G000100.1; TraesCLE_scaffold_165303_01G000100.1; TraesCLE_scaffold_165303_01G000100.
DR EnsemblPlants; TraesCS7A02G325400.1; TraesCS7A02G325400.1.cds1; TraesCS7A02G325400.
DR EnsemblPlants; TraesCS7B02G226100.1; TraesCS7B02G226100.1.cds1; TraesCS7B02G226100.
DR EnsemblPlants; TraesPAR_scaffold_002487_01G000400.1; TraesPAR_scaffold_002487_01G000400.1; TraesPAR_scaffold_002487_01G000400.
DR EnsemblPlants; TraesPAR_scaffold_187407_01G000100.1; TraesPAR_scaffold_187407_01G000100.1; TraesPAR_scaffold_187407_01G000100.
DR EnsemblPlants; TraesROB_scaffold_003895_01G000100.1; TraesROB_scaffold_003895_01G000100.1; TraesROB_scaffold_003895_01G000100.
DR EnsemblPlants; TraesROB_scaffold_166817_01G000100.1; TraesROB_scaffold_166817_01G000100.1; TraesROB_scaffold_166817_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_000640_01G000600.1; TraesWEE_scaffold_000640_01G000600.1; TraesWEE_scaffold_000640_01G000600.
DR EnsemblPlants; TraesWEE_scaffold_120293_01G000100.1; TraesWEE_scaffold_120293_01G000100.1; TraesWEE_scaffold_120293_01G000100.
DR Gramene; TraesCAD_scaffold_002919_01G000100.1; TraesCAD_scaffold_002919_01G000100.1; TraesCAD_scaffold_002919_01G000100.
DR Gramene; TraesCAD_scaffold_134402_01G000100.1; TraesCAD_scaffold_134402_01G000100.1; TraesCAD_scaffold_134402_01G000100.
DR Gramene; TraesCAD_scaffold_166582_01G000100.1; TraesCAD_scaffold_166582_01G000100.1; TraesCAD_scaffold_166582_01G000100.
DR Gramene; TraesCLE_scaffold_001556_01G000100.1; TraesCLE_scaffold_001556_01G000100.1; TraesCLE_scaffold_001556_01G000100.
DR Gramene; TraesCLE_scaffold_165303_01G000100.1; TraesCLE_scaffold_165303_01G000100.1; TraesCLE_scaffold_165303_01G000100.
DR Gramene; TraesCS7A02G325400.1; TraesCS7A02G325400.1.cds1; TraesCS7A02G325400.
DR Gramene; TraesCS7B02G226100.1; TraesCS7B02G226100.1.cds1; TraesCS7B02G226100.
DR Gramene; TraesPAR_scaffold_002487_01G000400.1; TraesPAR_scaffold_002487_01G000400.1; TraesPAR_scaffold_002487_01G000400.
DR Gramene; TraesPAR_scaffold_187407_01G000100.1; TraesPAR_scaffold_187407_01G000100.1; TraesPAR_scaffold_187407_01G000100.
DR Gramene; TraesROB_scaffold_003895_01G000100.1; TraesROB_scaffold_003895_01G000100.1; TraesROB_scaffold_003895_01G000100.
DR Gramene; TraesROB_scaffold_166817_01G000100.1; TraesROB_scaffold_166817_01G000100.1; TraesROB_scaffold_166817_01G000100.
DR Gramene; TraesWEE_scaffold_000640_01G000600.1; TraesWEE_scaffold_000640_01G000600.1; TraesWEE_scaffold_000640_01G000600.
DR Gramene; TraesWEE_scaffold_120293_01G000100.1; TraesWEE_scaffold_120293_01G000100.1; TraesWEE_scaffold_120293_01G000100.
DR eggNOG; ENOG502S3RJ; Eukaryota.
DR OMA; CAARMIS; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P00228; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:486088"
FT CHAIN 47..143
FT /note="Ferredoxin, chloroplastic"
FT /id="PRO_0000008840"
FT DOMAIN 49..139
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 90
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 143 AA; 15286 MW; 4AF136605BD058FC CRC64;
MAAALSLRAP FSLRAVAPPA PRVALAPAAL SLAAAKQVRG ARLRAQATYK VKLVTPEGEV
ELEVPDDVYI LDQAEEEGID LPYSCRAGSC SSCAGKLVSG EIDQSDQSFL DDDQMEAGWV
LTCHAYPKSD IVIETHKEEE LTA