[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Kidney; PubMed=1371282 [NCBI, ExPASy, EBI, Israel, Japan] Fakhrai H., Maines M.D.; "Expression and characterization of a cDNA for rat kidney biliverdin reductase. Evidence suggesting the liver and kidney enzymes are the same transcript product."; J. Biol. Chem. 267:4023-4029(1992).
[2]	PROTEIN SEQUENCE OF 119-136, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.
[3]	MUTAGENESIS. PubMed=8020496 [NCBI, ExPASy, EBI, Israel, Japan] McCoubrey W.K. Jr., Maines M.D.; "Site-directed mutagenesis of cysteine residues in biliverdin reductase. Roles in substrate and cofactor binding."; Eur. J. Biochem. 222:597-603(1994).
[4]	CRYSTALLIZATION. DOI=10.1107/S0907444900008520; PubMed=10957639 [NCBI, ExPASy, EBI, Israel, Japan] Sun D., Sato M., Yoshida T., Shimizu H., Miyatake H., Adachi S., Shiro Y., Kikuchi A.; "Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase."; Acta Crystallogr. D 56:1180-1182(2000).
[5]	X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 8-291. DOI=10.1016/S0022-2836(02)00383-2; PubMed=12079357 [NCBI, ExPASy, EBI, Israel, Japan] Whitby F.G., Phillips J.D., Hill C.P., McCoubrey W.K. Jr., Maines M.D.; "Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex."; J. Mol. Biol. 319:1199-1210(2002).

Comments

FUNCTION: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
CATALYTIC ACTIVITY: Bilirubin + NAD(P)⁺ = biliverdin + NAD(P)H.
COFACTOR: Binds 1 zinc ion per subunit.
PATHWAY: Porphyrin metabolism; protoheme degradation .
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems.
SIMILARITY: Belongs to the gfo/idh/mocA family. Biliverdin reductase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M81681; AAA40830.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A42268; A42268.

NP_446302.1; -.

3D structure databases

PDB

1GCU; X-ray; 1.40 A; A=1-295.	[ExPASy / RCSB / EBI]
1LC0; X-ray; 1.20 A; A=8-295.	[ExPASy / RCSB / EBI]
1LC3; X-ray; 1.50 A; A=8-295.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GCU; -.
1LC0; -.
1LC3; -.

ModBase

P46844.

Organism-specific databases

RGD

620721; Blvra.

Gene expression databases

GermOnline

ENSRNOG00000011778; Rattus norvegicus.

Family and domain databases

InterPro

IPR017094; Biliverdin_Rdtase_A.
IPR015249; Biliverdin_Rdtase_cat.
IPR000683; GFO/IDH/MocA_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF09166; Biliv-reduc_cat; 1.
PF01408; GFO_IDH_MocA; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037032; Biliverdin_reductase_A; 1.

BLOCKS

P46844.

Genome annotation databases

Ensembl

ENSRNOG00000011778; Rattus norvegicus. [Contig view]

GeneID

116599; -.

KEGG

rno:116599; -.

Phylogenomic databases

HOVERGEN

P46844; -.

Other

ProtoNet

P46844.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; NADP; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 2`	`2`		`PRO_0000010856`
`CHAIN`	`3 295`	`293`	`Biliverdin reductase A.`	`PRO_0000010857`
`COMPBIAS`	`11 16`	`6`	`Poly-Val.`
`METAL`	`279 279`		`Zinc (Potential).`
`METAL`	`280 280`		`Zinc (Potential).`
`METAL`	`291 291`		`Zinc (Potential).`
`METAL`	`292 292`		`Zinc (Potential).`
`MUTAGEN`	`73 73`		`C->A: Loss of activity.`
`MUTAGEN`	`280 280`		`C->A: Reduced activity.`
`MUTAGEN`	`291 291`		`C->A: Reduced activity.`
`STRAND`	`7 14`	`8`
`HELIX`	`18 27`	`10`
`HELIX`	`30 33`	`4`
`STRAND`	`36 42`	`7`
`STRAND`	`53 55`	`3`
`HELIX`	`58 63`	`6`
`STRAND`	`69 72`	`4`
`HELIX`	`76 78`	`3`
`HELIX`	`79 88`	`10`
`STRAND`	`92 97`	`6`
`HELIX`	`103 116`	`14`
`STRAND`	`120 123`	`4`
`HELIX`	`125 128`	`4`
`HELIX`	`130 139`	`10`
`STRAND`	`144 153`	`10`
`HELIX`	`158 161`	`4`
`HELIX`	`164 167`	`4`
`HELIX`	`169 179`	`11`
`STRAND`	`183 192`	`10`
`HELIX`	`193 195`	`3`
`STRAND`	`197 205`	`9`
`STRAND`	`211 218`	`8`
`STRAND`	`225 232`	`8`
`STRAND`	`235 237`	`3`
`HELIX`	`249 261`	`13`
`HELIX`	`267 291`	`25`

Sequence information

Length: 295 AA [This is the length of the unprocessed precursor]

Molecular weight: 33566 Da [This is the MW of the unprocessed precursor]

CRC64: 219C8EA96C150588 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDAEPKRKFG VVVVGVGRAG SVRLRDLKDP RSAAFLNLIG FVSRRELGSL DEVRQISLED 

        70         80         90        100        110        120 
ALRSQEIDVA YICSESSSHE DYIRQFLQAG KHVLVEYPMT LSFAAAQELW ELAAQKGRVL 

       130        140        150        160        170        180 
HEEHVELLME EFEFLRREVL GKELLKGSLR FTASPLEEER FGFPAFSGIS RLTWLVSLFG 

       190        200        210        220        230        240 
ELSLISATLE ERKEDQYMKM TVQLETQNKG LLSWIEEKGP GLKRNRYVNF QFTSGSLEEV 

       250        260        270        280        290 
PSVGVNKNIF LKDQDIFVQK LLDQVSAEDL AAEKKRIMHC LGLASDIQKL CHQKK

P46844 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools