NB5R1_ARATH
ID NB5R1_ARATH Reviewed; 281 AA.
AC Q9ZNT1; Q93YQ9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=NADH--cytochrome b5 reductase 1 {ECO:0000303|PubMed:17227547};
DE EC=1.6.2.2 {ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378};
GN Name=CBR1 {ECO:0000303|PubMed:17227547};
GN Synonyms=CBR {ECO:0000303|PubMed:9880378};
GN OrderedLocusNames=At5g17770 {ECO:0000312|Araport:AT5G17770};
GN ORFNames=MVA3.13 {ECO:0000312|EMBL:BAB09576.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9880378; DOI=10.1104/pp.119.1.353;
RA Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
RT "Microsomal electron transfer in higher plants: cloning and heterologous
RT expression of NADH-cytochrome b5 reductase from Arabidopsis.";
RL Plant Physiol. 119:353-361(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 [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.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-78, AND NOMENCLATURE.
RX PubMed=17227547; DOI=10.1111/j.1365-313x.2006.02925.x;
RA Kumar R., Wallis J.G., Skidmore C., Browse J.;
RT "A mutation in Arabidopsis cytochrome b5 reductase identified by high-
RT throughput screening differentially affects hydroxylation and
RT desaturation.";
RL Plant J. 48:920-932(2006).
RN [8]
RP INTERACTION WITH AKR2A.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [9]
RP AKR2A-BINDING SEQUENCE, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21896887; DOI=10.1104/pp.111.183160;
RA Duncan O., Taylor N.L., Carrie C., Eubel H., Kubiszewski-Jakubiak S.,
RA Zhang B., Narsai R., Millar A.H., Whelan J.;
RT "Multiple lines of evidence localize signaling, morphology, and lipid
RT biosynthesis machinery to the mitochondrial outer membrane of
RT Arabidopsis.";
RL Plant Physiol. 157:1093-1113(2011).
CC -!- FUNCTION: Reductase transferring electrons from NADH to cytochrome b5.
CC Required for the NADH-dependent electron transfer involved in the
CC desaturation and hydroxylation of fatty acids and in the desaturation
CC of sterol precursors. No activity with NADPH as electron donor.
CC {ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC Evidence={ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46681;
CC Evidence={ECO:0000269|PubMed:17227547, ECO:0000269|PubMed:9880378};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P83686};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for NADH {ECO:0000269|PubMed:9880378};
CC -!- SUBUNIT: Monomer. Interacts with AKR2A (PubMed:20215589). {ECO:0000250,
CC ECO:0000269|PubMed:20215589}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21896887}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21896887}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and siliques.
CC Detected in leaves. {ECO:0000269|PubMed:9880378}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL24304.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB007799; BAA74837.1; -; mRNA.
DR EMBL; AB007800; BAA74838.1; -; Genomic_DNA.
DR EMBL; AB006706; BAB09576.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92466.1; -; Genomic_DNA.
DR EMBL; AY059822; AAL24304.1; ALT_FRAME; mRNA.
DR EMBL; AY072482; AAL66897.1; -; mRNA.
DR EMBL; AK316787; BAH19505.1; -; mRNA.
DR EMBL; AY085728; AAM62946.1; -; mRNA.
DR PIR; T52470; T52470.
DR RefSeq; NP_197279.1; NM_121783.5.
DR AlphaFoldDB; Q9ZNT1; -.
DR SMR; Q9ZNT1; -.
DR BioGRID; 16921; 3.
DR STRING; 3702.AT5G17770.1; -.
DR PaxDb; Q9ZNT1; -.
DR PRIDE; Q9ZNT1; -.
DR ProteomicsDB; 251248; -.
DR EnsemblPlants; AT5G17770.1; AT5G17770.1; AT5G17770.
DR GeneID; 831645; -.
DR Gramene; AT5G17770.1; AT5G17770.1; AT5G17770.
DR KEGG; ath:AT5G17770; -.
DR Araport; AT5G17770; -.
DR TAIR; locus:2176001; AT5G17770.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_2_1; -.
DR InParanoid; Q9ZNT1; -.
DR OMA; KDMRFSF; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q9ZNT1; -.
DR BioCyc; ARA:AT5G17770-MON; -.
DR PRO; PR:Q9ZNT1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZNT1; baseline and differential.
DR Genevisible; Q9ZNT1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:TAIR.
DR GO; GO:0022900; P:electron transport chain; IDA:TAIR.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..281
FT /note="NADH--cytochrome b5 reductase 1"
FT /id="PRO_0000419622"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..149
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT MOTIF 34..40
FT /note="AKR2A-binding sequence (ABS) required for
FT mitochondrion outer membrane targeting"
FT /evidence="ECO:0000269|PubMed:21057222"
FT BINDING 129..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 155..187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P83291"
FT MUTAGEN 78
FT /note="L->F: In cbr1-1; decreased stability and decreased
FT activity."
FT /evidence="ECO:0000269|PubMed:17227547"
SQ SEQUENCE 281 AA; 31490 MW; E6654D95FEA2BCD2 CRC64;
MDTEFLRTLD RQILLGVFVA FVAVGAGAAY FLTSSKKRRV CLDPENFKEF KLVKRHQLSH
NVAKFVFELP TSTSVLGLPI GQHISCRGKD GQGEDVIKPY TPTTLDSDVG RFELVIKMYP
QGRMSHHFRE MRVGDHLAVK GPKGRFKYQP GQFRAFGMLA GGSGITPMFQ VARAILENPT
DKTKVHLIYA NVTYDDILLK EELEGLTTNY PEQFKIFYVL NQPPEVWDGG VGFVSKEMIQ
THCPAPASDI QILRCGPPPM NKAMAANLEA LGYSPEMQFQ F
