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Protein

Biliverdin reductase A

Gene

Blvra

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi: protoheme degradation

This protein is involved in the pathway protoheme degradation, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway protoheme degradation and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei97NAD or NADP; via carbonyl oxygen1 Publication1
Metal bindingi279ZincSequence analysis1
Metal bindingi280ZincSequence analysis1
Metal bindingi291ZincSequence analysis1
Metal bindingi292ZincSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 20NAD or NADP1 Publication6
Nucleotide bindingi76 – 79NAD or NADP1 Publication4

GO - Molecular functioni

  • biliverdin reductase activity Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BRENDAi1.3.1.24. 5301.
SABIO-RKP46844.
UniPathwayiUPA00684.

Names & Taxonomyi

Protein namesi
Recommended name:
Biliverdin reductase A (EC:1.3.1.24)
Short name:
BVR A
Alternative name(s):
Biliverdin-IX alpha-reductase
Gene namesi
Name:Blvra
Synonyms:Blvr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620721. Blvra.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73C → A: Loss of activity. 1 Publication1
Mutagenesisi280C → A: Reduced activity. 1 Publication1
Mutagenesisi291C → A: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000108561 – 22
ChainiPRO_00000108573 – 295Biliverdin reductase AAdd BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei154PhosphoserineCombined sources1
Modified residuei173PhosphothreonineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei247N6-acetyllysineBy similarity1
Modified residuei252N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP46844.
PRIDEiP46844.

PTM databases

iPTMnetiP46844.
PhosphoSitePlusiP46844.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015843.

Structurei

Secondary structure

1295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 14Combined sources7
Helixi18 – 27Combined sources10
Helixi30 – 33Combined sources4
Beta strandi36 – 42Combined sources7
Beta strandi53 – 55Combined sources3
Helixi58 – 63Combined sources6
Beta strandi65 – 72Combined sources8
Helixi76 – 78Combined sources3
Helixi79 – 88Combined sources10
Beta strandi92 – 97Combined sources6
Helixi103 – 115Combined sources13
Beta strandi120 – 123Combined sources4
Helixi125 – 128Combined sources4
Helixi130 – 139Combined sources10
Beta strandi144 – 154Combined sources11
Helixi158 – 161Combined sources4
Helixi164 – 167Combined sources4
Helixi169 – 179Combined sources11
Beta strandi183 – 192Combined sources10
Helixi193 – 195Combined sources3
Beta strandi197 – 205Combined sources9
Beta strandi211 – 218Combined sources8
Beta strandi225 – 234Combined sources10
Beta strandi235 – 237Combined sources3
Helixi249 – 261Combined sources13
Helixi267 – 290Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCUX-ray1.40A1-295[»]
1LC0X-ray1.20A5-295[»]
1LC3X-ray1.50A5-295[»]
ProteinModelPortaliP46844.
SMRiP46844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46844.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 16Poly-Val6

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiP46844.
KOiK00214.
PhylomeDBiP46844.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAEPKRKFG VVVVGVGRAG SVRLRDLKDP RSAAFLNLIG FVSRRELGSL
60 70 80 90 100
DEVRQISLED ALRSQEIDVA YICSESSSHE DYIRQFLQAG KHVLVEYPMT
110 120 130 140 150
LSFAAAQELW ELAAQKGRVL HEEHVELLME EFEFLRREVL GKELLKGSLR
160 170 180 190 200
FTASPLEEER FGFPAFSGIS RLTWLVSLFG ELSLISATLE ERKEDQYMKM
210 220 230 240 250
TVQLETQNKG LLSWIEEKGP GLKRNRYVNF QFTSGSLEEV PSVGVNKNIF
260 270 280 290
LKDQDIFVQK LLDQVSAEDL AAEKKRIMHC LGLASDIQKL CHQKK
Length:295
Mass (Da):33,566
Last modified:November 1, 1995 - v1
Checksum:i219C8EA96C150588
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81681 mRNA. Translation: AAA40830.1.
PIRiA42268.
RefSeqiNP_446302.1. NM_053850.1.
UniGeneiRn.9865.

Genome annotation databases

GeneIDi116599.
KEGGirno:116599.
UCSCiRGD:620721. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81681 mRNA. Translation: AAA40830.1.
PIRiA42268.
RefSeqiNP_446302.1. NM_053850.1.
UniGeneiRn.9865.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCUX-ray1.40A1-295[»]
1LC0X-ray1.20A5-295[»]
1LC3X-ray1.50A5-295[»]
ProteinModelPortaliP46844.
SMRiP46844.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015843.

PTM databases

iPTMnetiP46844.
PhosphoSitePlusiP46844.

Proteomic databases

PaxDbiP46844.
PRIDEiP46844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116599.
KEGGirno:116599.
UCSCiRGD:620721. rat.

Organism-specific databases

CTDi644.
RGDi620721. Blvra.

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiP46844.
KOiK00214.
PhylomeDBiP46844.

Enzyme and pathway databases

UniPathwayiUPA00684.
BRENDAi1.3.1.24. 5301.
SABIO-RKP46844.

Miscellaneous databases

EvolutionaryTraceiP46844.
PROiP46844.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBIEA_RAT
AccessioniPrimary (citable) accession number: P46844
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.