ID   NB5R2_XENTR             Reviewed;         304 AA.
AC   Q5BJ68;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            Short=b5R.2;
DE            EC=1.6.2.2;
GN   Name=cyb5r2; ORFNames=TNeu132f07.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) 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; CR942741; CAJ83022.1; -; mRNA.
DR   EMBL; BC091602; AAH91602.1; -; mRNA.
DR   RefSeq; NP_001025638.1; NM_001030467.1.
DR   AlphaFoldDB; Q5BJ68; -.
DR   SMR; Q5BJ68; -.
DR   PaxDb; Q5BJ68; -.
DR   DNASU; 595026; -.
DR   GeneID; 595026; -.
DR   KEGG; xtr:595026; -.
DR   CTD; 51700; -.
DR   Xenbase; XB-GENE-1006041; cyb5r2.
DR   eggNOG; KOG0534; Eukaryota.
DR   HOGENOM; CLU_003827_9_2_1; -.
DR   InParanoid; Q5BJ68; -.
DR   OMA; NKHDHIA; -.
DR   OrthoDB; 1311668at2759; -.
DR   TreeFam; TF314333; -.
DR   Reactome; R-XTR-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000009054; Expressed in mesonephros and 11 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:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0001878; P:response to yeast; IEA:Ensembl.
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..304
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000287554"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..155
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         135..150
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  33745 MW;  0790DEB00965A0A6 CRC64;
     MEISTDSNML VALAVIGVTV LLFLIKALGS QAKKAPLTLL DPNAKYPLPL IEKQEISHDT
     KKFRFGLPSQ EHVLGLPVGQ HVYLSAKING SLVVRAYTPV SSDEVKGHVD LIVKVYYKNV
     HPKFPEGGKM SQHLDSLKIG ETIDFRGPNG LLVYKEKGKF AIRPDKKSEP KLKVAKHVGM
     LAGGTGITPM LQLIRQITQD PNDNTKCSLI FANQTEDDIL LRYELETVAK SHPEQFKLWY
     TLDRPPQGWK YGAGFVTADM IKEHLPPPSE DVVVLMCGPP PMIQFACQDN LTKLGYPEAG
     RFAY