A3MWK6 · DHE4_PYRCJ
- ProteinNADP(+)-dependent glutamate dehydrogenase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP+/NADPH as the acceptor/donor over NAD+/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2-aminobutyrate, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.
Catalytic activity
- H2O + L-glutamate + NADP+ = 2-oxoglutarate + H+ + NADPH + NH4+
Activity regulation
Is not regulated allosterically. Activity is inhibited in the presence of high ionic strength; the inhibitory effect of KCl is slightly higher than that of NaCl.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.035 mM | NADP+ | 50 | ||||
3.4 mM | L-glutamate | 50 | ||||
0.017 mM | NADPH | 50 | ||||
1.7 mM | 2-oxoglutarate | 50 | ||||
2.2 mM | ammonia | 50 |
kcat is 13 sec-1 for oxidative deamination of L-glutamate, and 95 sec-1 for reductive amination of 2-oxoglutarate (at 50 degrees Celsius).
pH Dependence
Optimum pH is 9.5 for oxidative deamination, and 9.0 for reductive amination. Retains more than 80% of its activity after incubation for 30 minutes at pH 4.5-9.5.
Temperature Dependence
Optimum temperature is 90 degrees Celsius for oxidative deamination. Retains full activity after incubation for 10 minutes at temperatures up to 90 degrees Celsius.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 70 | substrate | ||||
Sequence: K | ||||||
Binding site | 94 | substrate | ||||
Sequence: K | ||||||
Active site | 106 | Proton donor | ||||
Sequence: K | ||||||
Site | 146 | Important for catalysis | ||||
Sequence: D | ||||||
Binding site | 190 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 221 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 354 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glutamate dehydrogenase (NAD+) activity | |
Molecular Function | glutamate dehydrogenase (NADP+) activity | |
Molecular Function | NADP+ binding | |
Molecular Function | NADPH binding | |
Biological Process | 2-oxoglutarate metabolic process | |
Biological Process | glutamate catabolic process | |
Biological Process | glutamate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADP(+)-dependent glutamate dehydrogenase
- EC number
- Short namesNADP-GDH
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionA3MWK6
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000432228 | 1-421 | NADP+-dependent glutamate dehydrogenase | |||
Sequence: MSQNGQFLEYTLQVIRRGVEMGGFPEDFYKLLSRPKRIIQVSIPVKMDNGSYEVFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSKLAGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIEGKTVAVHGAGNTGAWAAYWLEKMGAKVVAISDTRGTVVNKAGIPGEQILKVYMEKKRDKSATVLALEGEKIADSNASLYQDVDILVPAAIENVVREDNVGLVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI |
Expression
Induction
Is constitutively expressed.
Interaction
Structure
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)46,610
- Last updated2007-04-03 v1
- ChecksumDECEAEB7942AE122
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000561 EMBL· GenBank· DDBJ | ABO09023.1 EMBL· GenBank· DDBJ | Genomic DNA |