Q94JV5 · NILP2_ARATH
- ProteinDeaminated glutathione amidase, chloroplastic/cytosolic
- GeneNLP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids307 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione (PubMed:30692244).
Possesses amidase activity toward deaminated ophthalmate in vitro (PubMed:30692244).
Possesses amidase activity toward deaminated ophthalmate in vitro (PubMed:30692244).
Catalytic activity
- N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = L-cysteinylglycine + 2-oxoglutarateThis reaction proceeds in the forward direction.
- N-(4-carboxy-4-oxobutanoyl)-L-ethylglycylglycine + H2O = N-(2-aminobutanoyl)glycine + 2-oxoglutarateThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
35 μM | N-(4-oxoglutarate)-L-cysteinylglycine | |||||
6.7 μM | ophthalmate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
7.9 μmol/min/mg | with N-(4-oxoglutarate)-L-cysteinylglycine as substrate | ||||
5.6 μmol/min/mg | with ophthalmate as substrate |
kcat is 4.2 sec-1 with N-(4-oxoglutarate)-L-cysteinylglycine as substrate (PubMed:30692244).
kcat is 3.0 sec-1 with ophthalmate as substrate (PubMed:30692244).
kcat is 3.0 sec-1 with ophthalmate as substrate (PubMed:30692244).
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 76 | Proton acceptor | |||
Active site | 147 | Proton donor | |||
Active site | 188 | Nucleophile | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | cytoplasm | |
Cellular Component | plastid | |
Molecular Function | [acetyl-CoA carboxylase]-phosphatase activity | |
Molecular Function | deaminated glutathione amidase activity | |
Biological Process | metabolite repair |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDeaminated glutathione amidase, chloroplastic/cytosolic
- EC number
- Short namesdGSH amidase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94JV5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Isoform 2
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but the accumuluation of N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione) in mutant plants is up to 70-fold higher than in the wild type.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 29 | No cytoplasmic localization. | |||
Variants
![](/variants.8e7f84.jpg)
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 34 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-36 | Chloroplast | |||
Chain | PRO_0000426705 | 37-307 | Deaminated glutathione amidase, chloroplastic/cytosolic | ||
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 37-286 | CN hydrolase | |||
Sequence similarities
Belongs to the nitrilase superfamily. NIT1/NIT2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative initiation.
Q94JV5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsFull-length, FL
- Length307
- Mass (Da)33,971
- Last updated2001-12-01 v1
- MD5 Checksum5C1A8D3161CC346FE72EFC20D5177A66
Q94JV5-2
- Name2
- SynonymsTruncated, Tr
- Differences from canonical
- 1-28: Missing
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_060389 | 1-28 | in isoform 2 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL161512 EMBL· GenBank· DDBJ | CAB78004.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161813 EMBL· GenBank· DDBJ | CAB82115.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE82678.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF372904 EMBL· GenBank· DDBJ | AAK49620.1 EMBL· GenBank· DDBJ | mRNA | ||
AY133544 EMBL· GenBank· DDBJ | AAM91374.1 EMBL· GenBank· DDBJ | mRNA |