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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NAD or NADP; via carbonyl oxygen1 Publication
Metal bindingi279 – 2791ZincSequence analysis
Metal bindingi280 – 2801ZincSequence analysis
Metal bindingi291 – 2911ZincSequence analysis
Metal bindingi292 – 2921ZincSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 206NAD or NADP1 Publication
Nucleotide bindingi76 – 794NAD or NADP1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731C → A: Loss of activity. 1 Publication
Mutagenesisi280 – 2801C → A: Reduced activity. 1 Publication
Mutagenesisi291 – 2911C → A: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22PRO_0000010856
Chaini3 – 295293Biliverdin reductase APRO_0000010857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei173 – 1731PhosphothreonineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei247 – 2471N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP46844.
PRIDEiP46844.

PTM databases

iPTMnetiP46844.
PhosphoSiteiP46844.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015843.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Helixi18 – 2710Combined sources
Helixi30 – 334Combined sources
Beta strandi36 – 427Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 636Combined sources
Beta strandi65 – 728Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8810Combined sources
Beta strandi92 – 976Combined sources
Helixi103 – 11513Combined sources
Beta strandi120 – 1234Combined sources
Helixi125 – 1284Combined sources
Helixi130 – 13910Combined sources
Beta strandi144 – 15411Combined sources
Helixi158 – 1614Combined sources
Helixi164 – 1674Combined sources
Helixi169 – 17911Combined sources
Beta strandi183 – 19210Combined sources
Helixi193 – 1953Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi225 – 23410Combined sources
Beta strandi235 – 2373Combined sources
Helixi249 – 26113Combined sources
Helixi267 – 29024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GCUX-ray1.40A1-295[»]
1LC0X-ray1.20A5-295[»]
1LC3X-ray1.50A5-295[»]
ProteinModelPortaliP46844.
SMRiP46844. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46844.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 166Poly-Val

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1GCUX-ray1.40A1-295[»]
1LC0X-ray1.20A5-295[»]
1LC3X-ray1.50A5-295[»]
ProteinModelPortaliP46844.
SMRiP46844. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015843.

PTM databases

iPTMnetiP46844.
PhosphoSiteiP46844.

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: June 8, 2016
This is version 129 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.