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
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
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 Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. Reduced riboflavin + NADP(+) = riboflavin + NADPH. 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
15846
18009
17607
17033
16908
16474
17015
15378
PubChem 5280352
5893
5886
14080393
439153
5884
493570
1038
1hdoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAP Unbound Unbound Unbound Unbound Unbound
1he2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAP Unbound Bound:BLA Unbound Unbound Unbound
1he3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAP Unbound Analogue:MBV Unbound Unbound Unbound
1he4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAP Unbound Unbound Unbound Unbound Analogue:FMN
1he5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1he2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1he3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1he4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1he5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

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, conformation, and enzymatic reduction in biliverdins.
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, an early fetal bilirubin IXbeta producing enzyme.
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. Structure-activity relationships define models for both active sites.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-02-04 2009-02-26