FER4_ARATH
ID FER4_ARATH Reviewed; 148 AA.
AC Q9FIA7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable ferredoxin-4, chloroplastic;
DE Short=AtFd4;
DE Flags: Precursor;
GN Name=FD4; OrderedLocusNames=At5g10000; ORFNames=MYH9.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=14684843; DOI=10.1104/pp.103.032755;
RA Hanke G.T., Kimata-Ariga Y., Taniguchi I., Hase T.;
RT "A post genomic characterization of Arabidopsis ferredoxins.";
RL Plant Physiol. 134:255-264(2004).
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; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -152 mV. {ECO:0000269|PubMed:14684843};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. Not detected in roots.
CC {ECO:0000269|PubMed:14684843}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AB016893; BAB09421.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91480.1; -; Genomic_DNA.
DR RefSeq; NP_196562.1; NM_121038.1.
DR AlphaFoldDB; Q9FIA7; -.
DR SMR; Q9FIA7; -.
DR STRING; 3702.AT5G10000.1; -.
DR PaxDb; Q9FIA7; -.
DR PRIDE; Q9FIA7; -.
DR ProteomicsDB; 228902; -.
DR EnsemblPlants; AT5G10000.1; AT5G10000.1; AT5G10000.
DR GeneID; 830862; -.
DR Gramene; AT5G10000.1; AT5G10000.1; AT5G10000.
DR KEGG; ath:AT5G10000; -.
DR Araport; AT5G10000; -.
DR TAIR; locus:2178153; AT5G10000.
DR eggNOG; ENOG502RZ87; Eukaryota.
DR HOGENOM; CLU_082632_1_1_1; -.
DR InParanoid; Q9FIA7; -.
DR OMA; CCILESA; -.
DR OrthoDB; 1486602at2759; -.
DR PhylomeDB; Q9FIA7; -.
DR PRO; PR:Q9FIA7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIA7; 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; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..148
FT /note="Probable ferredoxin-4, chloroplastic"
FT /id="PRO_0000322571"
FT DOMAIN 54..145
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 148 AA; 16255 MW; 0F669EF5CD35736E CRC64;
MDQVLYSSYI IKIPVISRIS PSQAQLTTRL NNTTYFGLSS SRGNFGKVFA KESRKVKLIS
PEGEEQEIEG NEDCCILESA ENAGLELPYS CRSGTCGTCC GKLVSGKVDQ SLGSFLEEEQ
IQKGYILTCI ALPLEDCVVY THKQSDLI
