FER2_ARATH
ID FER2_ARATH Reviewed; 148 AA.
AC P16972; Q0WWH2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ferredoxin-2, chloroplastic;
DE Short=AtFd2;
DE Flags: Precursor;
GN Name=FD2; Synonyms=PETF, PETF1; OrderedLocusNames=At1g60950;
GN ORFNames=T7P1.9;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2102830; DOI=10.1007/bf00027495;
RA Vorst O., van Dam F., Oosterhoff-Teertstra R., Smeekens S., Weisbeek P.;
RT "Tissue-specific expression directed by an Arabidopsis thaliana pre-
RT ferredoxin promoter in transgenic tobacco plants.";
RL Plant Mol. Biol. 14:491-499(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16667505; DOI=10.1104/pp.93.2.572;
RA Somers D.E., Caspar T., Quail P.H.;
RT "Isolation and characterization of a ferredoxin gene from Arabidopsis
RT thaliana.";
RL Plant Physiol. 93:572-577(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH PGRL1A AND PGRL1B.
RC STRAIN=cv. Columbia;
RX PubMed=18243102; DOI=10.1016/j.cell.2007.12.028;
RA DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D.,
RA Finazzi G., Joliot P., Barbato R., Leister D.;
RT "A complex containing PGRL1 and PGR5 is involved in the switch between
RT linear and cyclic electron flow in Arabidopsis.";
RL Cell 132:273-285(2008).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -433 mV. {ECO:0000269|PubMed:14684843};
CC -!- SUBUNIT: Interacts with PGRL1A and PGRL1B.
CC {ECO:0000269|PubMed:18243102}.
CC -!- INTERACTION:
CC P16972; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-449431, EBI-15193683;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; X51370; CAA35754.1; -; Genomic_DNA.
DR EMBL; M35868; AAA32790.1; -; mRNA.
DR EMBL; AC018908; AAG51652.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33752.1; -; Genomic_DNA.
DR EMBL; AF324706; AAG40057.1; -; mRNA.
DR EMBL; AF326885; AAG41467.1; -; mRNA.
DR EMBL; AF339705; AAK00387.1; -; mRNA.
DR EMBL; AY093034; AAM13033.1; -; mRNA.
DR EMBL; AY128936; AAM91336.1; -; mRNA.
DR EMBL; AK226379; BAE98526.1; -; mRNA.
DR PIR; S09979; S09979.
DR RefSeq; NP_176291.1; NM_104775.3.
DR PDB; 4ZHO; X-ray; 2.34 A; A/B=52-145.
DR PDB; 6B03; X-ray; 2.70 A; C/F=53-145.
DR PDB; 6B05; X-ray; 1.90 A; B/C=53-145.
DR PDB; 6BRS; X-ray; 2.30 A; C/F=53-145.
DR PDBsum; 4ZHO; -.
DR PDBsum; 6B03; -.
DR PDBsum; 6B05; -.
DR PDBsum; 6BRS; -.
DR AlphaFoldDB; P16972; -.
DR SASBDB; P16972; -.
DR SMR; P16972; -.
DR BioGRID; 27610; 12.
DR IntAct; P16972; 4.
DR STRING; 3702.AT1G60950.1; -.
DR PaxDb; P16972; -.
DR PRIDE; P16972; -.
DR ProteomicsDB; 230775; -.
DR EnsemblPlants; AT1G60950.1; AT1G60950.1; AT1G60950.
DR GeneID; 842386; -.
DR Gramene; AT1G60950.1; AT1G60950.1; AT1G60950.
DR KEGG; ath:AT1G60950; -.
DR Araport; AT1G60950; -.
DR TAIR; locus:2206061; AT1G60950.
DR eggNOG; ENOG502RXFZ; Eukaryota.
DR HOGENOM; CLU_082632_1_1_1; -.
DR InParanoid; P16972; -.
DR OMA; AYPRSNC; -.
DR OrthoDB; 1557921at2759; -.
DR PhylomeDB; P16972; -.
DR PRO; PR:P16972; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P16972; baseline and differential.
DR Genevisible; P16972; AT.
DR GO; GO:0009507; C:chloroplast; 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 GO; GO:0009643; P:photosynthetic acclimation; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
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; 3D-structure; Chloroplast; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT CHAIN 53..148
FT /note="Ferredoxin-2, chloroplastic"
FT /id="PRO_0000008825"
FT DOMAIN 55..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"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6B05"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6B05"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:6B05"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4ZHO"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:4ZHO"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4ZHO"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4ZHO"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4ZHO"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6B05"
SQ SEQUENCE 148 AA; 15539 MW; 0E7EF445BEB23F62 CRC64;
MASTALSSAI VGTSFIRRSP APISLRSLPS ANTQSLFGLK SGTARGGRVT AMATYKVKFI
TPEGELEVEC DDDVYVLDAA EEAGIDLPYS CRAGSCSSCA GKVVSGSVDQ SDQSFLDDEQ
IGEGFVLTCA AYPTSDVTIE THKEEDIV
