A0A0K0JBQ6 · A0A0K0JBQ6_BRUMA
- ProteinGMP reductase
- Genebma-gmpr-1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids364 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Catalytic activity
- IMP + NH4+ + NADP+ = GMP + NADPH + 2 H+
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-27 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: SR | ||||||
Binding site | 78 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: K | ||||||
Binding site | 132-134 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: DVA | ||||||
Binding site | 184 | K+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 186 | K+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 189 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 189 | K+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 191 | Proton donor/acceptor | ||||
Sequence: T | ||||||
Binding site | 192 | K+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 222-224 | GMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 245-246 | GMP (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 271-273 | GMP (UniProtKB | ChEBI) | ||||
Sequence: GMA | ||||||
Binding site | 272 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: M | ||||||
Binding site | 288-289 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: YR | ||||||
Binding site | 289-293 | GMP (UniProtKB | ChEBI) | ||||
Sequence: RASEG | ||||||
Binding site | 317-320 | NADP+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: SACT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | GMP reductase complex | |
Molecular Function | GMP reductase activity | |
Molecular Function | metal ion binding | |
Biological Process | purine nucleobase metabolic process | |
Biological Process | purine nucleotide metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGMP reductase
- EC number
- Short namesGMPR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Spiruromorpha > Filarioidea > Onchocercidae > Brugia
Accessions
- Primary accessionA0A0K0JBQ6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-343 | IMP dehydrogenase/GMP reductase | ||||
Sequence: LDFKDVLLRPKRSTLKSRADVDLVREFIFRNSKKKYVGIPVIASNMDTVGTFEVAEVLSKKKLFTFIHKHYSVEQWVEFVSRTDSNQDTMSQIGISSGVSDFDFAKLKEICGLIPELQYICLDVANGYTEMFVDFIRRVREGFPRHTIFAGNVVTGEMIEELILSGVDVVKVGLGPGSVCTTRKKTGVGYPQLSAVLECADAAHGLNGHVVSDGGCTNPGDVAKAFGAGADFVMIGGLFAGHDQCGGDTVVKDGQKYKLFYGMASDTAMKRHEGSVAEYRASEGKTITLPCRGDISDTVQDLLGGLRSACTYTGAKKLKELSKRATFVRVTQQT |
Sequence similarities
Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length364
- Mass (Da)40,032
- Last updated2015-10-14 v1
- Checksum31E4800A7ACEBC1E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN856924 EMBL· GenBank· DDBJ | CTP81075.1 EMBL· GenBank· DDBJ | Genomic DNA |