MFDR_ARATH
ID MFDR_ARATH Reviewed; 483 AA.
AC Q8W3L1; O49356;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial;
DE Short=Adrenodoxin reductase {ECO:0000303|PubMed:12714594};
DE EC=1.18.1.6 {ECO:0000269|PubMed:13677469};
DE AltName: Full=Mitochondrial ferredoxin reductase;
DE Short=AtMFDR {ECO:0000303|PubMed:13677469};
DE Flags: Precursor;
GN Name=MFDR {ECO:0000303|PubMed:13677469};
GN Synonyms=ADXR {ECO:0000303|PubMed:12714594};
GN OrderedLocusNames=At4g32360 {ECO:0000312|Araport:AT4G32360};
GN ORFNames=F10M6.10 {ECO:0000312|EMBL:CAA16955.1},
GN F8B4.60 {ECO:0000312|EMBL:CAA22563.1};
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:BAB79228.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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).
CC -!- FUNCTION: Associates in vitro with the adrenodoxin-like protein MFDX1
CC to form an efficient low potential electron transfer chain that is able
CC to 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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC Evidence={ECO:0000269|PubMed:13677469};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:13677469};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 uM for NADPH {ECO:0000269|PubMed:12714594};
CC KM=11.3 uM for NADPH {ECO:0000269|PubMed:13677469};
CC KM=123 uM for NADH {ECO:0000269|PubMed:13677469};
CC KM=1000 uM for NADH {ECO:0000269|PubMed:12714594};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:13677469}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16955.1; Type=Erroneous gene model prediction;
CC Sequence=CAA22563.1; Type=Erroneous gene model prediction;
CC Sequence=CAB79953.1; Type=Erroneous gene model prediction;
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DR EMBL; AY074927; AAL82814.1; -; mRNA.
DR EMBL; AB075740; BAB79228.1; -; mRNA.
DR EMBL; AL021811; CAA16955.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL034567; CAA22563.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79953.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86046.1; -; Genomic_DNA.
DR PIR; T05346; T05346.
DR RefSeq; NP_194962.2; NM_119388.5.
DR AlphaFoldDB; Q8W3L1; -.
DR SMR; Q8W3L1; -.
DR BioGRID; 14656; 1.
DR STRING; 3702.AT4G32360.1; -.
DR PaxDb; Q8W3L1; -.
DR PRIDE; Q8W3L1; -.
DR EnsemblPlants; AT4G32360.1; AT4G32360.1; AT4G32360.
DR GeneID; 829370; -.
DR Gramene; AT4G32360.1; AT4G32360.1; AT4G32360.
DR KEGG; ath:AT4G32360; -.
DR Araport; AT4G32360; -.
DR TAIR; locus:2127811; AT4G32360.
DR eggNOG; KOG1800; Eukaryota.
DR HOGENOM; CLU_024722_3_0_1; -.
DR InParanoid; Q8W3L1; -.
DR OMA; RFNFIGN; -.
DR OrthoDB; 1324510at2759; -.
DR PhylomeDB; Q8W3L1; -.
DR BioCyc; ARA:AT4G32360-MON; -.
DR BRENDA; 2.8.1.6; 399.
DR SABIO-RK; Q8W3L1; -.
DR PRO; PR:Q8W3L1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W3L1; baseline and differential.
DR Genevisible; Q8W3L1; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
PE 1: Evidence at protein level;
KW Biotin biosynthesis; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW NADP; Oxidoreductase; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..483
FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial"
FT /id="PRO_0000430544"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 169..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 213..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 398..400
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 398
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
SQ SEQUENCE 483 AA; 53070 MW; 25B7B47DDF8A8A19 CRC64;
MSRYLARYMV SRYFSSASSR PLHVCIVGSG PAGFYTADKV LKAHEGAHVD IIDRLPTPFG
LVRSGVAPDH PETKIAINQF SRVAQHERCS FIGNVKLGSD LSLSELRDLY HVVVLAYGAE
SDKDLGIPGE SLSGIYSARE FVWWYNGHPD YSSLKPDLKT SDSAVILGQG NVALDVARIL
LRPTTELAST DIATHALSAL KESSIRKVYL IGRRGPVQAA LTAKELREVL GIKNLHIRIK
QTDLSVTPAD EEEMKTSRAR KRIYELLSKA AAAAKTSEAD PDQRELHFVF FRQPDQFLES
DERKGHVSGV NLQKTILESV GTGKQIAVGT GEFEDLNCSM VLKAIGYKSV PVNGLPFDHK
KGVVPNVKGR VVSHTSGDIS QTEPGLYVCG WLKRGPVGII ATNLYCAEET VGSISEDIEE
GVWKSSKAGS KGLMQLLEKR KVKKVEFSGW EKIDAKEKQM GIERNKPREK LVTWEDLLAA
AAN
