FER3_ARATH
ID FER3_ARATH Reviewed; 155 AA.
AC Q9ZQG8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ferredoxin-3, chloroplastic;
DE Short=AtFd3;
DE Flags: Precursor;
GN Name=FD3; OrderedLocusNames=At2g27510; ORFNames=F10A12.19;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY NITRATE.
RX PubMed=10948265; DOI=10.2307/3871145;
RA Wang R., Guegler K., LaBrie S.T., Crawford N.M.;
RT "Genomic analysis of a nutrient response in Arabidopsis reveals diverse
RT expression patterns and novel metabolic and potential regulatory genes
RT induced by nitrate.";
RL Plant Cell 12:1491-1509(2000).
RN [6]
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-50, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -337 mV. {ECO:0000269|PubMed:14684843};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:14684843}.
CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:10948265}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AC006232; AAD15602.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08008.1; -; Genomic_DNA.
DR EMBL; AY086622; AAM63681.1; -; mRNA.
DR EMBL; BT004187; AAO42206.1; -; mRNA.
DR EMBL; BT005393; AAO63813.1; -; mRNA.
DR PIR; G84673; G84673.
DR RefSeq; NP_180320.1; NM_128311.3.
DR AlphaFoldDB; Q9ZQG8; -.
DR SMR; Q9ZQG8; -.
DR BioGRID; 2649; 2.
DR STRING; 3702.AT2G27510.1; -.
DR iPTMnet; Q9ZQG8; -.
DR PaxDb; Q9ZQG8; -.
DR PRIDE; Q9ZQG8; -.
DR ProteomicsDB; 230416; -.
DR EnsemblPlants; AT2G27510.1; AT2G27510.1; AT2G27510.
DR GeneID; 817297; -.
DR Gramene; AT2G27510.1; AT2G27510.1; AT2G27510.
DR KEGG; ath:AT2G27510; -.
DR Araport; AT2G27510; -.
DR TAIR; locus:2038593; AT2G27510.
DR eggNOG; ENOG502S3RJ; Eukaryota.
DR HOGENOM; CLU_082632_1_2_1; -.
DR InParanoid; Q9ZQG8; -.
DR OMA; CEIQTHK; -.
DR OrthoDB; 1527635at2759; -.
DR PhylomeDB; Q9ZQG8; -.
DR PRO; PR:Q9ZQG8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQG8; baseline and differential.
DR Genevisible; Q9ZQG8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; Acetylation; Chloroplast; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 50..155
FT /note="Ferredoxin-3, chloroplastic"
FT /id="PRO_0000322570"
FT DOMAIN 61..152
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MOD_RES 50
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 155 AA; 16634 MW; 07BA87E39B29F221 CRC64;
MATVRISSTS MTKAVLRSQT TNKLITNKSY NLSVGSTKRV SRSFGLKCSA NSGGATMSAV
YKVKLLGPDG QEDEFEVQDD QYILDAAEEA GVDLPYSCRA GACSTCAGQI VSGNVDQSDG
SFLEDSHLEK GYVLTCVAYP QSDCVIHTHK ETELF
