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Identification
HMDB Protein ID HMDBP00701
Secondary Accession Numbers
  • 5974
  • HMDBP04878
Name Flavin reductase (NADPH)
Synonyms
  1. BVR-B
  2. Biliverdin reductase B
  3. Biliverdin-IX beta-reductase
  4. FLR
  5. FR
  6. GHBP
  7. Green heme-binding protein
  8. NADPH-dependent diaphorase
  9. NADPH-flavin reductase
Gene Name BLVRB
Protein Type Unknown
Biological Properties
General Function Involved in catalytic activity
Specific 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.
Pathways
  • Porphyrin and chlorophyll metabolism
  • Riboflavin metabolism
Reactions
Riboflavin reduced + NADP → Riboflavin + NADPH details
Bilirubin + NAD(P)(+) → Biliverdin + NAD(P)H details
Bilirubin + NAD → Biliverdin + NADH + Hydrogen Ion details
Bilirubin + NADP → Biliverdin + NADPH + Hydrogen Ion details
Riboflavin reduced + NADP → Riboflavin + NADPH + Hydrogen Ion details
FAD + NADPH + Hydrogen Ion → FADH + NADP details
GO Classification
Biological Process
small molecule metabolic process
heme catabolic process
Cellular Component
cytosol
plasma membrane
nucleus
Function
binding
catalytic activity
Molecular Function
biliverdin reductase activity
riboflavin reductase (NADPH) activity
nucleotide binding
Process
metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 19
Locus 19q13.1-q13.2
SNPs BLVRB
Gene Sequence
>621 bp
ATGGCCGTCAAGAAGATCGCGATCTTCGGCGCCACTGGCCAGACCGGGCTCACCACCCTG
GCGCAGGCGGTGCAAGCAGGTTACGAAGTGACAGTGCTGGTGCGGGACTCCTCCAGGCTG
CCATCAGAGGGGCCCCGGCCGGCCCACGTGGTAGTGGGAGATGTTCTGCAGGCAGCCGAT
GTGGACAAGACCGTGGCTGGGCAGGACGCTGTCATCGTGCTGCTGGGCACCCGCAATGAC
CTCAGTCCCACGACAGTGATGTCCGAGGGCGCCCGGAACATTGTGGCAGCCATGAAGGCT
CATGGTGTGGACAAGGTCGTGGCCTGCACCTCGGCTTTCCTGCTCTGGGACCCTACCAAG
GTGCCCCCACGACTGCAGGCTGTGACTGATGACCACATCCGGATGCACAAGGTGCTGCGG
GAATCAGGCCTGAAGTACGTGGCTGTGATGCCGCCACACATAGGAGACCAGCCACTAACT
GGGGCGTACACAGTGACCCTGGATGGACGAGGGCCCTCAAGGGTCATCTCCAAACATGAC
CTGGGCCATTTCATGCTGCGCTGCCTCACCACCGATGAGTACGACGGACACAGCACCTAC
CCCTCCCACCAGTACCAGTAG
Protein Properties
Number of Residues 206
Molecular Weight 22119.215
Theoretical pI 7.643
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Flavin reductase
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAAD
VDKTVAGQDAVIVLLGTRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTK
VPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHD
LGHFMLRCLTTDEYDGHSTYPSHQYQ
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P30043
UniProtKB/Swiss-Prot Entry Name BLVRB_HUMAN
PDB IDs
GenBank Gene ID D26308
GeneCard ID BLVRB
GenAtlas ID BLVRB
HGNC ID HGNC:1063
References
General References
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  6. Yamaguchi T, Komoda Y, Nakajima H: Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. J Biol Chem. 1994 Sep 30;269(39):24343-8. [PubMed:7929092 ]
  7. Chikuba K, Yubisui T, Shirabe K, Takeshita M: Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1170-6. [PubMed:8117274 ]
  8. Komuro A, Tobe T, Hashimoto K, Nakano Y, Yamaguchi T, Nakajima H, Tomita M: Molecular cloning and expression of human liver biliverdin-IX beta reductase. Biol Pharm Bull. 1996 Jun;19(6):796-804. [PubMed:8799475 ]
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