EzCatDB: S00335
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DB codeS00335
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.3.1.24,1.5.1.30

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

P30043
Protein nameFlavin reductasebiliverdin 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)

SynonymsFR
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
RefSeqNP_000704.1 (Protein)
NM_000713.2 (DNA/RNA sequence)

KEGG pathways
MAP codePathwaysE.C.
MAP00860Porphyrin and chlorophyll metabolism1.3.1.24

UniProtKB:Accession NumberP30043
Entry nameBLVRB_HUMAN
ActivityReduced riboflavin + NADP(+) = riboflavin + NADPH.,Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
SubunitMonomer.
Subcellular locationCytoplasm (Potential).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00486C00003C00006C01007C00500C00004C00005C00255C00080
E.C.1.3.1.241.3.1.241.3.1.24,1.5.1.301.5.1.301.3.1.241.3.1.241.3.1.24,1.5.1.301.5.1.301.3.1.24,1.5.1.30
CompoundBilirubinNAD+NADP+Reduced riboflavinBiliverdinNADHNADPHRiboflavinH+
Typeamide group,aromatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrateamide group,aromatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrateothers
ChEBI16990
15846
18009
17607
17033
16908
16474
17015
15378
PubChem5280352
5893
5886
14080393

439153
5884
493570
1038
                 
1hdoAUnboundUnboundBound:NAPUnboundUnboundUnboundUnboundUnbound 
1he2AUnboundUnboundBound:NAPUnboundBound:BLAUnboundUnboundUnbound 
1he3AUnboundUnboundBound:NAPUnboundAnalogue:MBVUnboundUnboundUnbound 
1he4AUnboundUnboundBound:NAPUnboundUnboundUnboundUnboundAnalogue:FMN 
1he5AUnboundUnboundBound:NAPUnboundUnboundUnboundUnboundAnalogue:LUM 

Active-site residues
pdb
        
1hdoA
1he2A
1he3A
1he4A
1he5A

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.4
[6]p.217
[7]Fig8, p.1205-1206

references
[1]
PubMed ID2393401
JournalBiochem Biophys Res Commun
Year1990
Volume171
Pages465-73
AuthorsFrydman RB, Bari S, Tomaro ML, Frydman B
TitleThe enzymatic and chemical reduction of extended biliverdins.
[2]
PubMed ID1417867
JournalBiochem Biophys Res Commun
Year1992
Volume188
Pages48-56
AuthorsBari S, Frydman RB, Grosman C, Frydman B
TitleThe interplay between basicity, conformation, and enzymatic reduction in biliverdins.
[3]
PubMed ID8253726
JournalJ Biol Chem
Year1993
Volume268
Pages26099-106
AuthorsTerry MJ, Maines MD, Lagarias JC
TitleInactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase.
[4]
PubMed ID9359830
JournalBiochem J
Year1997
Volume328
Pages33-6
AuthorsEnnis O, Maytum R, Mantle TJ
TitleCloning 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.
[5]
PubMed ID11224558
JournalNat Struct Biol
Year2001
Volume8
Pages198-200
AuthorsMcDonagh AF
TitleTurning green to gold.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS)
Medline ID21127483
PubMed ID11224564
JournalNat Struct Biol
Year2001
Volume8
Pages215-20
AuthorsPereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M
TitleStructure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme.
Related PDB1hdo,1he2,1he3,1he4,1he5
Related UniProtKBP30043
[7]
PubMed ID12079357
JournalJ Mol Biol
Year2002
Volume319
Pages1199-210
AuthorsWhitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD
TitleCrystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
[8]
PubMed ID10858451
JournalJ Biol Chem
Year2000
Volume275
Pages19009-17
AuthorsCunningham O, Dunne A, Sabido P, Lightner D, Mantle TJ
TitleStudies 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.


createdupdated
2004-02-042009-02-26


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