MFDX2_ARATH
ID MFDX2_ARATH Reviewed; 197 AA.
AC Q8S904; O49551;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adrenodoxin-like protein 2, mitochondrial {ECO:0000303|PubMed:12714594};
DE AltName: Full=Mitochondrial ferredoxin 2 {ECO:0000303|PubMed:13677469};
DE Short=AtMFDX2 {ECO:0000303|PubMed:13677469};
DE Flags: Precursor;
GN Name=MFDX2 {ECO:0000303|PubMed:13677469};
GN Synonyms=ADX2 {ECO:0000303|PubMed:12714594};
GN OrderedLocusNames=At4g21090 {ECO:0000312|Araport:AT4G21090};
GN ORFNames=F7J7.30 {ECO:0000312|EMBL:CAA17528.1};
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 {ECO:0000312|EMBL:BAB86773.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=12714594; DOI=10.1074/jbc.m302154200;
RA Picciocchi A., Douce R., Alban C.;
RT "The plant biotin synthase reaction. Identification and characterization of
RT essential mitochondrial accessory protein components.";
RL J. Biol. Chem. 278:24966-24975(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=13677469; DOI=10.1023/a:1025015811141;
RA Takubo K., Morikawa T., Nonaka Y., Mizutani M., Takenaka S., Takabe K.,
RA Takahashi M.A., Ohta D.;
RT "Identification and molecular characterization of mitochondrial ferredoxins
RT and ferredoxin reductase from Arabidopsis.";
RL Plant Mol. Biol. 52:817-830(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
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.
CC -!- FUNCTION: Associates with the adrenodoxin reductase MFDR to form an
CC efficient low potential electron transfer chain that is able to reduce
CC cytochrome C. {ECO:0000250|UniProtKB:Q9M0V0}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9M0V0}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17528.1; Type=Erroneous gene model prediction;
CC Sequence=CAB79109.1; Type=Erroneous gene model prediction;
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DR EMBL; AY074925; AAL82812.1; -; mRNA.
DR EMBL; AB075739; BAB79227.1; -; mRNA.
DR EMBL; AB081937; BAB86773.1; -; mRNA.
DR EMBL; AL021960; CAA17528.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79109.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84398.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84399.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84400.1; -; Genomic_DNA.
DR EMBL; BT004804; AAO44070.1; -; mRNA.
DR EMBL; AK317477; BAH20142.1; -; mRNA.
DR EMBL; AK227833; BAE99811.1; -; mRNA.
DR PIR; T04940; T04940.
DR RefSeq; NP_001031685.1; NM_001036608.1.
DR RefSeq; NP_193841.2; NM_118227.4.
DR RefSeq; NP_849415.1; NM_179084.2.
DR AlphaFoldDB; Q8S904; -.
DR SMR; Q8S904; -.
DR STRING; 3702.AT4G21090.2; -.
DR PaxDb; Q8S904; -.
DR PRIDE; Q8S904; -.
DR ProteomicsDB; 232277; -.
DR EnsemblPlants; AT4G21090.1; AT4G21090.1; AT4G21090.
DR EnsemblPlants; AT4G21090.2; AT4G21090.2; AT4G21090.
DR EnsemblPlants; AT4G21090.3; AT4G21090.3; AT4G21090.
DR GeneID; 827856; -.
DR Gramene; AT4G21090.1; AT4G21090.1; AT4G21090.
DR Gramene; AT4G21090.2; AT4G21090.2; AT4G21090.
DR Gramene; AT4G21090.3; AT4G21090.3; AT4G21090.
DR KEGG; ath:AT4G21090; -.
DR Araport; AT4G21090; -.
DR TAIR; locus:2127358; AT4G21090.
DR eggNOG; KOG3309; Eukaryota.
DR HOGENOM; CLU_082632_0_0_1; -.
DR InParanoid; Q8S904; -.
DR OMA; HYLQSSA; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; Q8S904; -.
DR BRENDA; 2.8.1.6; 399.
DR PRO; PR:Q8S904; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8S904; baseline and differential.
DR Genevisible; Q8S904; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
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; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..74
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 75..197
FT /note="Adrenodoxin-like protein 2, mitochondrial"
FT /id="PRO_0000430543"
FT DOMAIN 81..184
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 165
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 197 AA; 22121 MW; E06F3BEACCA6292B CRC64;
MVFHRLSRLG SRIVKELPRE RHLSMCGKRI LQRSYGQYLQ SSPMLQRQTR SFKEALFSNN
HKFCTSFSTT SEKGGEKTEK INVTFVDKDG EEIHIKVPVG MNILEAAHEN DIELEGACEG
SLACSTCHVI VMDTKYYNKL EEPTDEENDM LDLAFGLTAT SRLGCQVIAK PELDGVRLAI
PSATRNFAVD GFVPKPH
