MFDX1_ARATH
ID MFDX1_ARATH Reviewed; 197 AA.
AC Q9M0V0; Q8LDZ8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Adrenodoxin-like protein 1, mitochondrial {ECO:0000303|PubMed:12714594};
DE AltName: Full=Mitochondrial ferredoxin 1 {ECO:0000303|PubMed:13677469};
DE Short=AtMFDX1 {ECO:0000303|PubMed:13677469};
DE Flags: Precursor;
GN Name=MFDX1 {ECO:0000303|PubMed:13677469};
GN Synonyms=ADX1 {ECO:0000303|PubMed:12714594};
GN OrderedLocusNames=At4g05450 {ECO:0000312|Araport:AT4G05450};
GN ORFNames=C6L9.130;
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 [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBCELLULAR LOCATION.
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], FUNCTION, AND SUBCELLULAR LOCATION.
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].
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.
CC -!- FUNCTION: Associates in vitro with the adrenodoxin reductase MFDR to
CC form an efficient low potential electron transfer chain that is able to
CC reduce cytochrome C (PubMed:12714594, PubMed:13677469). Functions as
CC accessory mitochondrial protein involved with BIO2 in the plant biotin
CC synthase reaction (PubMed:12714594). {ECO:0000269|PubMed:12714594,
CC ECO:0000269|PubMed:13677469}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- INTERACTION:
CC Q9M0V0; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-25517302, EBI-15193683;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:12714594, ECO:0000269|PubMed:13677469}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; AY074926; AAL82813.1; -; mRNA.
DR EMBL; AB075738; BAB79226.1; -; mRNA.
DR EMBL; AL161503; CAB81087.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82522.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68073.1; -; Genomic_DNA.
DR EMBL; AY065280; AAL38756.1; -; mRNA.
DR EMBL; AY091324; AAM14263.1; -; mRNA.
DR EMBL; AY085707; AAM62925.1; -; mRNA.
DR PIR; E85068; E85068.
DR RefSeq; NP_001329852.1; NM_001340554.1.
DR RefSeq; NP_192454.1; NM_116784.4.
DR AlphaFoldDB; Q9M0V0; -.
DR SMR; Q9M0V0; -.
DR BioGRID; 11206; 1.
DR IntAct; Q9M0V0; 1.
DR STRING; 3702.AT4G05450.1; -.
DR PaxDb; Q9M0V0; -.
DR PRIDE; Q9M0V0; -.
DR ProteomicsDB; 250620; -.
DR EnsemblPlants; AT4G05450.1; AT4G05450.1; AT4G05450.
DR EnsemblPlants; AT4G05450.2; AT4G05450.2; AT4G05450.
DR GeneID; 825895; -.
DR Gramene; AT4G05450.1; AT4G05450.1; AT4G05450.
DR Gramene; AT4G05450.2; AT4G05450.2; AT4G05450.
DR KEGG; ath:AT4G05450; -.
DR Araport; AT4G05450; -.
DR TAIR; locus:2115939; AT4G05450.
DR eggNOG; KOG3309; Eukaryota.
DR HOGENOM; CLU_082632_0_0_1; -.
DR InParanoid; Q9M0V0; -.
DR OMA; CHVILPD; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; Q9M0V0; -.
DR BioCyc; ARA:AT4G05450-MON; -.
DR BRENDA; 2.8.1.6; 399.
DR SABIO-RK; Q9M0V0; -.
DR PRO; PR:Q9M0V0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0V0; baseline and differential.
DR Genevisible; Q9M0V0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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:0009102; P:biotin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0048868; P:pollen tube development; 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; 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 1: Evidence at protein level;
KW 2Fe-2S; Biotin biosynthesis; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..197
FT /note="Adrenodoxin-like protein 1, mitochondrial"
FT /id="PRO_0000430542"
FT DOMAIN 79..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"
FT CONFLICT 133
FT /note="D -> H (in Ref. 6; AAM62925)"
SQ SEQUENCE 197 AA; 21831 MW; A35325C9F8C40A85 CRC64;
MIGHRISRLG STIVKQLARE GYLATYGTKN LHRSYGHYLQ SLPVVPRQAR TSQEAWFLKS
HKFCTSSTTS SENGDEETEK ITIIFVDKDG EEIPVKVPIG MSVLEAAHEN DIDLEGACEA
SLACSTCHVI VMDTEYYNKL EEPTDEENDM LDLAFGLTET SRLGCQVIAR PELDGVRLAI
PSATRNFAVD GFVPKPH
