BLVRB
entrez
645
canonical
uniprot
P30043
canonical
ensembl
ENSG00000090013
resolver
ensp
ENSP00000263368
resolver
enst
ENST00000263368
resolver
genesymbol
BLVRB
resolver
genesymbol
HEL-S-10
resolver
genesymbol_syn
FLR
resolver
genesymbol_syn
SCAN
resolver
hgnc
HGNC:1063
resolver
uniprot
A6NKD8
resolver
uniprot
B2R5C6
resolver
uniprot
P32078
resolver
uniprot
P53005
resolver
uniprot
Q32LZ2
resolver
uniprot
V9HWI1
resolver
uniprot_entry
BLVRB_HUMAN
resolver
uniprot_entry
V9HWI1_HUMAN
resolver
uniprot_sec
A6NKD8
resolver
uniprot_sec
B2R5C6
resolver
uniprot_sec
P32078
resolver
uniprot_sec
P53005
resolver
uniprot_sec
Q32LZ2
resolver
activity_regulation
ACTIVITY REGULATION: Mesobiliverdin acts as a competitive inhibitor for flavin reduction, indicating that flavin and tetrapyrrole substrates compete for the same site (PubMed:10620517). Inhibited by a wide range of xanthene-based drugs, such as phloxine B, erythrosin B, tamibarotene, sulfasalazine, olsalazine, febuxostat, ataluren (PTC124) and deferasirox (PubMed:29487133, PubMed:34957824). {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:34957824}.
uniprot
proteins
amino_acid_sequence
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLGTRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ
uniprot
proteins
ec_number
1.3.1.-
uniprot
proteins
ec_number
1.5.1.30
uniprot
proteins
ec_number
2.6.99.-
uniprot
proteins
function
FUNCTION: Enzyme that can both act as a NAD(P)H-dependent reductase and a S-nitroso-CoA-dependent nitrosyltransferase (PubMed:10620517, PubMed:18241201, PubMed:27207795, PubMed:38056462, PubMed:7929092). Promotes fetal heme degradation during development (PubMed:10858451, PubMed:18241201, PubMed:7929092). Also expressed in adult tissues, where it acts as a regulator of hematopoiesis, intermediary metabolism (glutaminolysis, glycolysis, TCA cycle and pentose phosphate pathway) and insulin signaling (PubMed:27207795, PubMed:29500232, PubMed:38056462). Has a broad specificity oxidoreductase activity by catalyzing the NAD(P)H-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone) (PubMed:10620517, PubMed:18241201, PubMed:7929092). Contributes to fetal heme catabolism by catalyzing reduction of biliverdin IXbeta into bilirubin IXbeta in the liver (PubMed:10858451, PubMed:18241201, PubMed:7929092). Biliverdin IXbeta, which constitutes the major heme catabolite in the fetus is not present in adult (PubMed:10858451, PubMed:18241201, PubMed:7929092). Does not reduce bilirubin IXalpha (PubMed:10858451, PubMed:18241201, PubMed:7929092). Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH (PubMed:10620517). Acts as a protein nitrosyltransferase by catalyzing nitrosylation of cysteine residues of target proteins, such as HMOX2, INSR and IRS1 (PubMed:38056462). S-nitroso-CoA-dependent nitrosyltransferase activity is mediated via a 'ping-pong' mechanism: BLVRB first associates with both S-nitroso-CoA and protein substrate, nitric oxide group is then transferred from S-nitroso-CoA to Cys-109 and Cys-188 residues of BLVRB and from S-nitroso-BLVRB to the protein substrate (PubMed:38056462). Inhibits insulin signaling by mediating nitrosylation of INSR and IRS1, leading to their inhibition (PubMed:38056462). {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:10858451, ECO:0000269|PubMed:18241201, ECO:0000269|PubMed:27207795, ECO:0000269|PubMed:29500232, ECO:0000269|PubMed:38056462, ECO:0000269|PubMed:7929092}.
uniprot
proteins
mass_dalton
22119
uniprot
proteins
mutagenesis
MUTAGEN 14..16; /note="QTG->NAA: Abolished binding to NAD(P)H and S-nitroso-CoA, leading to abolished NAD(P)H-dependent reductase and a S-nitroso-CoA-dependent nitrosyltransferase activities."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 14; /note="Q->R: Increased affinity for coenzyme A."; /evidence="ECO:0000269|PubMed:32246827"; MUTAGEN 78; /note="R->A: Induces both an increase in active site micro-millisecond motions and an increase in the rate constants of coenzyme-binding."; /evidence="ECO:0000269|PubMed:29932944"; MUTAGEN 78; /note="R->G: Decreased affinity for coenzyme A."; /evidence="ECO:0000269|PubMed:32246827"; MUTAGEN 109; /note="C->R: Abolished S-nitroso-CoA-dependent nitrosyltransferase activity; when associated with R-188."; /evidence="ECO:0000269|PubMed:38056462"; MUTAGEN 111; /note="S->A: Abolished NAD(P)H-dependent reductase activity."; /evidence="ECO:0000269|PubMed:27897348"; MUTAGEN 153; /note="H->A: Reduced affinity for biliverdin."; /evidence="ECO:0000269|PubMed:18241201"; MUTAGEN 188; /note="C->R: Abolished S-nitroso-CoA-dependent nitrosyltransferase activity; when associated with R-109."; /evidence="ECO:0000269|PubMed:38056462
uniprot
proteins
protein_family
BLVRB family
uniprot
proteins
pubmed
10620517
uniprot
proteins
pubmed
10858451
uniprot
proteins
pubmed
11224564
uniprot
proteins
pubmed
1286669
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18241201
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27207795
uniprot
proteins
pubmed
27897348
uniprot
proteins
pubmed
29487133
uniprot
proteins
pubmed
29500232
uniprot
proteins
pubmed
29932944
uniprot
proteins
pubmed
32246827
uniprot
proteins
pubmed
34957824
uniprot
proteins
pubmed
37645217
uniprot
proteins
pubmed
38056462
uniprot
proteins
pubmed
7929092
uniprot
proteins
pubmed
8117274
uniprot
proteins
pubmed
8280170
uniprot
proteins
pubmed
8313871
uniprot
proteins
pubmed
8687377
uniprot
proteins
pubmed
8799475
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38056462, ECO:0000269|PubMed:7929092}.
uniprot
proteins