DB code: S00335
CATH domain | 3.40.50.720 : Rossmann fold | Catalytic domain |
---|---|---|
E.C. | 1.3.1.24 1.5.1.30 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq |
---|---|---|---|
P30043 |
Flavin reductase
|
FR
EC 1.5.1.30 NADPH-dependent diaphorase NADPH-flavin reductase FLR Biliverdin reductase B BVR-B EC 1.3.1.24 Biliverdin-IX beta-reductase Green heme-binding protein GHBP |
NP_000704.1
(Protein)
NM_000713.2 (DNA/RNA sequence) |
KEGG enzyme name |
---|
biliverdin reductase
(EC 1.3.1.24 ) flavin reductase (EC 1.5.1.30 ) NADPH:flavin oxidoreductase (EC 1.5.1.30 ) riboflavin mononucleotide (reduced nicotinamide adenine dinucleotidephosphate) reductase (EC 1.5.1.30 ) flavin mononucleotide reductase (EC 1.5.1.30 ) flavine mononucleotide reductase (EC 1.5.1.30 ) FMN reductase (NADPH) (EC 1.5.1.30 ) NADPH-dependent FMN reductase (EC 1.5.1.30 ) NADPH-flavin reductase (EC 1.5.1.30 ) NADPH-FMN reductase (EC 1.5.1.30 ) NADPH-specific FMN reductase (EC 1.5.1.30 ) riboflavin mononucleotide reductase (EC 1.5.1.30 ) riboflavine mononucleotide reductase (EC 1.5.1.30 ) NADPH2 dehydrogenase (flavin) (EC 1.5.1.30 ) NADPH2:riboflavin oxidoreductase (EC 1.5.1.30 ) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P30043 | BLVRB_HUMAN | Reduced riboflavin + NADP(+) = riboflavin + NADPH. Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. | Monomer. | Cytoplasm (Potential). |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00860 | Porphyrin and chlorophyll metabolism | 1.3.1.24 |
Compound table | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||||||
KEGG-id | C00486 | C00003 | C00006 | C01007 | C00500 | C00004 | C00005 | C00255 | C00080 | ||||||
E.C. |
1.3.1.24
|
1.3.1.24
|
1.3.1.24
1.5.1.30 |
1.5.1.30
|
1.3.1.24
|
1.3.1.24
|
1.3.1.24
1.5.1.30 |
1.5.1.30
|
1.3.1.24
1.5.1.30 |
||||||
Compound | Bilirubin | NAD+ | NADP+ | Reduced riboflavin | Biliverdin | NADH | NADPH | Riboflavin | H+ | ||||||
Type | amide group,aromatic ring (with nitrogen atoms),carboxyl group | amide group,amine group,nucleotide | amide group,amine group,nucleotide | amide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate | amide group,aromatic ring (with nitrogen atoms),carboxyl group | amide group,amine group,nucleotide | amide group,amine group,nucleotide | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate | others | ||||||
ChEBI |
16990 16990 |
15846 15846 |
18009 18009 |
17607 17607 |
17033 17033 |
16908 16908 |
16474 16474 |
17015 17015 |
15378 15378 |
||||||
PubChem |
5280352 5280352 |
5893 5893 |
5886 5886 |
14080393 14080393 |
439153 439153 |
5884 5884 |
493570 493570 |
1038 1038 |
|||||||
1hdoA | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1he2A | Unbound | Unbound | Bound:NAP | Unbound | Bound:BLA | Unbound | Unbound | Unbound | |||||||
1he3A | Unbound | Unbound | Bound:NAP | Unbound | Analogue:MBV | Unbound | Unbound | Unbound | |||||||
1he4A | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | Unbound | Analogue:FMN | |||||||
1he5A | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | Unbound | Analogue:LUM |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1hdoA | ||||||||||
1he2A | ||||||||||
1he3A | ||||||||||
1he4A | ||||||||||
1he5A |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[5]
|
Fig.4 | |
[6]
|
p.217 | |
[7]
|
Fig8, p.1205-1206 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2393401 |
Journal | Biochem Biophys Res Commun |
Year | 1990 |
Volume | 171 |
Pages | 465-73 |
Authors | Frydman RB, Bari S, Tomaro ML, Frydman B |
Title | The enzymatic and chemical reduction of extended biliverdins. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1417867 |
Journal | Biochem Biophys Res Commun |
Year | 1992 |
Volume | 188 |
Pages | 48-56 |
Authors | Bari S, Frydman RB, Grosman C, Frydman B |
Title |
The interplay between basicity, |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8253726 |
Journal | J Biol Chem |
Year | 1993 |
Volume | 268 |
Pages | 26099-106 |
Authors | Terry MJ, Maines MD, Lagarias JC |
Title | Inactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9359830 |
Journal | Biochem J |
Year | 1997 |
Volume | 328 |
Pages | 33-6 |
Authors | Ennis O, Maytum R, Mantle TJ |
Title | Cloning and overexpression of rat kidney biliverdin IX alpha reductase as a fusion protein with glutathione S-transferase: stereochemistry of NADH oxidation and evidence that the presence of the glutathione S-transferase domain does not effect BVR-A activity. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11224558 |
Journal | Nat Struct Biol |
Year | 2001 |
Volume | 8 |
Pages | 198-200 |
Authors | McDonagh AF |
Title | Turning green to gold. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) |
Medline ID | 21127483 |
PubMed ID | 11224564 |
Journal | Nat Struct Biol |
Year | 2001 |
Volume | 8 |
Pages | 215-20 |
Authors | Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M |
Title |
Structure of human biliverdin IXbeta reductase, |
Related PDB | 1hdo 1he2 1he3 1he4 1he5 |
Related UniProtKB | P30043 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12079357 |
Journal | J Mol Biol |
Year | 2002 |
Volume | 319 |
Pages | 1199-210 |
Authors | Whitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD |
Title | Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10858451 |
Journal | J Biol Chem |
Year | 2000 |
Volume | 275 |
Pages | 19009-17 |
Authors | Cunningham O, Dunne A, Sabido P, Lightner D, Mantle TJ |
Title |
Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-02-04 | 2009-02-26 |