P17649 · GABAT_YEAST
- Protein4-aminobutyrate aminotransferase
- GeneUGA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL).
Miscellaneous
Present with 573 molecules/cell in log phase SD medium.
Catalytic activity
- 2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.2 mM | 4-aminobutanoate | |||||
0.22 mM | 2-oxoglutarate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
12.8 μmol/min/mg |
pH Dependence
Optimum pH is 8.3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 135-136 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: GA | ||||||
Binding site | 192 | substrate | ||||
Sequence: R | ||||||
Binding site | 351 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | 4-aminobutyrate transaminase activity | |
Molecular Function | 4-aminobutyrate:2-oxoglutarate transaminase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | gamma-aminobutyric acid catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-aminobutyrate aminotransferase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP17649
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120382 | 1-471 | 4-aminobutyrate aminotransferase | |||
Sequence: MSICEQYYPEEPTKPTVKTESIPGPESQKQLKELGEVFDTRPAYFLADYEKSLGNYITDVDGNTYLDLYAQISSIALGYNNPALIKAAQSPEMIRALVDRPALGNFPSKDLDKILKQILKSAPKGQDHVWSGLSGADANELAFKAAFIYYRAKQRGYDADFSEKENLSVMDNDAPGAPHLAVLSFKRAFHGRLFASGSTTCSKPIHKLDFPAFHWPHAEYPSYQYPLDENSDANRKEDDHCLAIVEELIKTWSIPVAALIIEPIQSEGGDNHASKYFLQKLRDITLKYNVVYIIDEVQTGVGATGKLWCHEYADIQPPVDLVTFSKKFQSAGYFFHDPKFIPNKPYRQFNTWCGEPARMIIAGAIGQEISDKKLTEQCSRVGDYLFKKLEGLQKKYPENFQNLRGKGRGTFIAWDLPTGEKRDLLLKKLKLNGCNVGGCAVHAVRLRPSLTFEEKHADIFIEALAKSVNEL | ||||||
Modified residue | 326 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Induction
Subject to nitrogen catabolite repression. Expression is low in the presence of the preferred nitrogen sources, and up-regulated by GABA.
Structure
Sequence
- Sequence statusComplete
- Length471
- Mass (Da)52,946
- Last updated1996-10-01 v2
- Checksum33D446778A891F63
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 240 | in Ref. 1; CAA36833 and 2; ABF58895 | ||||
Sequence: H → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X52600 EMBL· GenBank· DDBJ | CAA36833.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ512723 EMBL· GenBank· DDBJ | ABF58895.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z72804 EMBL· GenBank· DDBJ | CAA97002.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692904 EMBL· GenBank· DDBJ | AAT92923.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA08115.1 EMBL· GenBank· DDBJ | Genomic DNA |