FDC2_ARATH
ID FDC2_ARATH Reviewed; 181 AA.
AC Q9C7Y4;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ferredoxin C 2, chloroplastic {ECO:0000303|PubMed:20966083};
DE Short=AtFdC2 {ECO:0000303|PubMed:20966083};
DE Flags: Precursor;
GN Name=FDC2 {ECO:0000303|PubMed:20966083};
GN OrderedLocusNames=At1g32550 {ECO:0000312|Araport:AT1G32550};
GN ORFNames=T9G5.4 {ECO:0000312|EMBL:AAG51248.1};
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=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 [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 GENE FAMILY.
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 [5]
RP INDUCTION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=20966083; DOI=10.1074/jbc.m110.161562;
RA Voss I., Goss T., Murozuka E., Altmann B., McLean K.J., Rigby S.E.J.,
RA Munro A.W., Scheibe R., Hase T., Hanke G.T.;
RT "FdC1, a novel ferredoxin protein capable of alternative electron
RT partitioning, increases in conditions of acceptor limitation at photosystem
RT I.";
RL J. Biol. Chem. 286:50-59(2011).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions (Probable). Mediates
CC alternative electron partitioning in conditions of acceptor limitation
CC at photosystem I (By similarity). {ECO:0000250|UniProtKB:O23344,
CC ECO:0000305}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:O23344}.
CC -!- INDUCTION: Slightly up-regulated in response to acceptor limitation at
CC photosystem I (PSI) in plants lacking of photosynthetic [2Fe-2S]
CC ferredoxin (Fd). {ECO:0000269|PubMed:20966083}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AC055769; AAG51248.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31501.1; -; Genomic_DNA.
DR EMBL; AY080800; AAL87281.1; -; mRNA.
DR EMBL; AY114079; AAM45127.1; -; mRNA.
DR PIR; A86451; A86451.
DR RefSeq; NP_174533.1; NM_102990.5.
DR AlphaFoldDB; Q9C7Y4; -.
DR SMR; Q9C7Y4; -.
DR STRING; 3702.AT1G32550.2; -.
DR PRIDE; Q9C7Y4; -.
DR ProteomicsDB; 230569; -.
DR EnsemblPlants; AT1G32550.1; AT1G32550.1; AT1G32550.
DR GeneID; 840149; -.
DR Gramene; AT1G32550.1; AT1G32550.1; AT1G32550.
DR KEGG; ath:AT1G32550; -.
DR Araport; AT1G32550; -.
DR PhylomeDB; Q9C7Y4; -.
DR PRO; PR:Q9C7Y4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7Y4; 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; 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; PS51085; 2FE2S_FER_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..181
FT /note="Ferredoxin C 2, chloroplastic"
FT /id="PRO_0000443799"
FT DOMAIN 59..151
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 181 AA; 20377 MW; 1AB6BB821FA36693 CRC64;
MALILPCTFC TSLQKKNFPI NRRYITNFRR GATTATCEFR IPVEVSTPSD RGSLVVPSHK
VTVHDRQRGV VHEFEVPEDQ YILHSAESQN ISLPFACRHG CCTSCAVRVK SGELRQPQAL
GISAELKSQG YALLCVGFPT SDLEVETQDE DEVYWLQFGR YFARGPIERD DYALELAMGD
E
