ID   NB5R2_XENLA             Reviewed;         296 AA.
AC   Q5PQA4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            Short=b5R.2;
DE            EC=1.6.2.2;
GN   Name=cyb5r2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation
CC       and elongation of fatty acids, cholesterol biosynthesis and drug
CC       metabolism. {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:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000305}.
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DR   EMBL; BC087294; AAH87294.1; -; mRNA.
DR   RefSeq; NP_001088670.1; NM_001095201.1.
DR   AlphaFoldDB; Q5PQA4; -.
DR   SMR; Q5PQA4; -.
DR   DNASU; 495932; -.
DR   GeneID; 495932; -.
DR   KEGG; xla:495932; -.
DR   CTD; 495932; -.
DR   Xenbase; XB-GENE-1006047; cyb5r2.S.
DR   OrthoDB; 1311668at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 495932; Expressed in liver and 14 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Membrane; NAD;
KW   Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..296
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000287553"
FT   TRANSMEM        2..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..147
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         127..142
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..201
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  32664 MW;  BC391EEE22573505 CRC64;
     MLVALAAIGV TVLLFLIKAL GSGAKKAPVT LLDPNAKYPL PLIEKQEISH DTKKFRFGLP
     SAEHVLGLPV GQHIYLSAKV NGSLVVRAYT PVSSDEVKGH VDLVVKVYYK NVNPKFPDGG
     KMSQHLDSLK IGETIDFRGP NGLLVYKGKG KFAIRPDKKA EPKIKVAKHV GMLAGGTGIT
     PMLQLIRQIT QDPNDNTKCY LIFANQTEDD ILLRYELETV AKSHPEQFKL WYTLDRPPQG
     WKYGSGFVTA DMIKEHLPPP SEDVLVLMCG PPPMIQFACQ DNLTKLGYPE AGRFAY