NB5R2_ARATH
ID NB5R2_ARATH Reviewed; 328 AA.
AC P83291; Q8LBD3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADH-cytochrome b5 reductase-like protein;
DE Short=B5R;
DE EC=1.6.2.2;
GN Name=CBR2; OrderedLocusNames=At5g20080; ORFNames=F28I16.230;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 61-74, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf {ECO:0000269|PubMed:11743114}, and
RC Stem {ECO:0000269|PubMed:11743114};
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP 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 [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Desaturation and elongation of fatty acids. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:21896887}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000250|UniProtKB:P36060}.
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DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92791.1; -; Genomic_DNA.
DR EMBL; AY087280; AAM64833.1; -; mRNA.
DR RefSeq; NP_568391.1; NM_122015.5.
DR AlphaFoldDB; P83291; -.
DR SMR; P83291; -.
DR BioGRID; 17406; 1.
DR STRING; 3702.AT5G20080.1; -.
DR iPTMnet; P83291; -.
DR PaxDb; P83291; -.
DR PRIDE; P83291; -.
DR ProteomicsDB; 251049; -.
DR EnsemblPlants; AT5G20080.1; AT5G20080.1; AT5G20080.
DR GeneID; 832130; -.
DR Gramene; AT5G20080.1; AT5G20080.1; AT5G20080.
DR KEGG; ath:AT5G20080; -.
DR Araport; AT5G20080; -.
DR TAIR; locus:2147680; AT5G20080.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_1_1; -.
DR InParanoid; P83291; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; P83291; -.
DR BioCyc; ARA:AT5G20080-MON; -.
DR PRO; PR:P83291; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P83291; baseline and differential.
DR Genevisible; P83291; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
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 Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..328
FT /note="NADH-cytochrome b5 reductase-like protein"
FT /id="PRO_0000167626"
FT DOMAIN 76..184
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
SQ SEQUENCE 328 AA; 35987 MW; 9C25F8EFBEA60E46 CRC64;
MATSFFRRLA RSAPITFPVA FGSQSKSGSG AFRFSTGAIA ALSGGFSYYY LTSGNNLVYL
DQAKEETGPK TALNPDKWLE FKLQDTARVS HNTQLFRFSF DPSAELGLHV ASCLLTRAPL
GYNAEGKTKY VIRPYTPISD PEAKGYFDLL IKVYPDGKMS QHFASLKPGD VLEVKGPVEK
FKYSPNMKKH IGMIAGGSGI TPMLQVIDAI VKNPEDNTQI SLLYANVSPD DILLKQKLDV
LQANHPNLKI FYTVDNPTKN WKGGVGYISK DMALKGLPLP TDDTLILVCG PPGMMEHISG
GKAPDWSQGE VKGILKELGY TEEMVFKF
