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Flavin reductase (NADPH) (FR) (EC 1.5.1.30) (Biliverdin reductase B) (BVR-B) (EC 1.3.1.24) (Biliverdin-IX beta-reductase) (Green heme-binding protein) (GHBP) (NADPH-dependent diaphorase) (NADPH-flavin reductase) (FLR)

 BLVRB_BOVIN             Reviewed;         206 AA.
P52556; Q3T0T4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
16-JAN-2019, entry version 120.
RecName: Full=Flavin reductase (NADPH);
Short=FR;
EC=1.5.1.30 {ECO:0000250|UniProtKB:P30043};
AltName: Full=Biliverdin reductase B;
Short=BVR-B;
EC=1.3.1.24 {ECO:0000250|UniProtKB:P30043};
AltName: Full=Biliverdin-IX beta-reductase;
AltName: Full=Green heme-binding protein;
Short=GHBP;
AltName: Full=NADPH-dependent diaphorase;
AltName: Full=NADPH-flavin reductase;
Short=FLR;
Name=BLVRB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-58 AND 118-127, AND
MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=7937764; DOI=10.1073/pnas.91.20.9322;
Quandt K.S., Hultquist D.E.;
"Flavin reductase: sequence of cDNA from bovine liver and tissue
distribution.";
Proc. Natl. Acad. Sci. U.S.A. 91:9322-9326(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-37; 121-137 AND 146-169.
TISSUE=Erythrocyte;
PubMed=2069570; DOI=10.1016/0006-291X(91)91816-U;
Quandt K.S., Xu F., Chen P., Hultquist D.E.;
"Evidence that the protein components of bovine erythrocyte green heme
binding protein and flavin reductase are identical.";
Biochem. Biophys. Res. Commun. 178:315-321(1991).
-!- FUNCTION: Broad specificity oxidoreductase that catalyzes the
NADPH-dependent reduction of a variety of flavins, such as
riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ
(pyrroloquinoline quinone). Contributes to heme catabolism and
metabolizes linear tetrapyrroles. Can also reduce the complexed
Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the
liver, converts biliverdin to bilirubin.
{ECO:0000250|UniProtKB:P30043}.
-!- CATALYTIC ACTIVITY:
Reaction=NADP(+) + reduced riboflavin = 2 H(+) + NADPH +
riboflavin; Xref=Rhea:RHEA:19377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17607, ChEBI:CHEBI:57783, ChEBI:CHEBI:57986,
ChEBI:CHEBI:58349; EC=1.5.1.30;
Evidence={ECO:0000250|UniProtKB:P30043};
-!- CATALYTIC ACTIVITY:
Reaction=bilirubin IXalpha + NAD(+) = biliverdin IXalpha + H(+) +
NADH; Xref=Rhea:RHEA:15797, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57977,
ChEBI:CHEBI:57991; EC=1.3.1.24;
Evidence={ECO:0000250|UniProtKB:P30043};
-!- CATALYTIC ACTIVITY:
Reaction=bilirubin IXalpha + NADP(+) = biliverdin IXalpha + H(+) +
NADPH; Xref=Rhea:RHEA:15793, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57783, ChEBI:CHEBI:57977, ChEBI:CHEBI:57991,
ChEBI:CHEBI:58349; EC=1.3.1.24;
Evidence={ECO:0000250|UniProtKB:P30043};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30043}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30043}.
-!- TISSUE SPECIFICITY: At least expressed in the liver and
erythrocyte.
-!- MASS SPECTROMETRY: Mass=21994; Method=Electrospray; Range=2-206;
Evidence={ECO:0000269|PubMed:7937764};
-----------------------------------------------------------------------
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EMBL; L35045; AAC37323.1; -; mRNA.
EMBL; BC102269; AAI02270.1; -; mRNA.
PIR; S68597; S68597.
RefSeq; NP_776676.1; NM_174251.1.
UniGene; Bt.4093; -.
ProteinModelPortal; P52556; -.
SMR; P52556; -.
STRING; 9913.ENSBTAP00000013889; -.
PaxDb; P52556; -.
PeptideAtlas; P52556; -.
PRIDE; P52556; -.
Ensembl; ENSBTAT00000013889; ENSBTAP00000013889; ENSBTAG00000010508.
GeneID; 281650; -.
KEGG; bta:281650; -.
CTD; 645; -.
VGNC; VGNC:26511; BLVRB.
eggNOG; ENOG410IXV9; Eukaryota.
eggNOG; ENOG4111JAS; LUCA.
GeneTree; ENSGT00390000014810; -.
HOGENOM; HOG000262432; -.
HOVERGEN; HBG050695; -.
InParanoid; P52556; -.
KO; K05901; -.
OMA; MTGECAV; -.
OrthoDB; 1166292at2759; -.
TreeFam; TF324063; -.
Reactome; R-BTA-189483; Heme degradation.
Proteomes; UP000009136; Chromosome 18.
Bgee; ENSBTAG00000010508; Expressed in 9 organ(s), highest expression level in spleen.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0004074; F:biliverdin reductase activity; ISS:UniProtKB.
GO; GO:0042602; F:riboflavin reductase (NADPH) activity; ISS:UniProtKB.
GO; GO:0042167; P:heme catabolic process; ISS:UniProtKB.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF13460; NAD_binding_10; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; NADP;
Oxidoreductase; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2069570}.
CHAIN 2 206 Flavin reductase (NADPH).
/FTId=PRO_0000064947.
NP_BIND 10 15 NADP. {ECO:0000250}.
NP_BIND 54 55 NADP. {ECO:0000250}.
NP_BIND 75 78 NADP. {ECO:0000250}.
BINDING 35 35 NADP. {ECO:0000250}.
BINDING 132 132 NADP. {ECO:0000250}.
BINDING 153 153 Substrate. {ECO:0000250}.
BINDING 154 154 NADP; via amide nitrogen. {ECO:0000250}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:P30043}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P30043}.
SEQUENCE 206 AA; 22132 MW; 79A679FED289E32C CRC64;
MVVKKIALFG ATGNTGLTTL AQAVQAGYEV TVLVRDPSRL PSEGPQPAHV VVGDVRQPAD
VDKTVAGQDA VIVLLGTRND LSPTTVMSEG AQNIVAAMKA HGVDKVVACT SAFLLWDPSK
VPPRLQDVTD DHIRMHKVLQ QSGLKYVAVM PPHIGDHPLT GAYTVTLDGR GPSRVISKHD
LGHFMLHCLT TDKYDGHTTY PSHVYE


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