P17649 · GABAT_YEAST

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

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
3.2 mM4-aminobutanoate
0.22 mM2-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.

TypeIDPosition(s)Description
Binding site135-136pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site192substrate
Binding site351pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Function4-aminobutyrate transaminase activity
Molecular Function4-aminobutyrate:2-oxoglutarate transaminase activity
Molecular Functionpyridoxal phosphate binding
Biological Processgamma-aminobutyric acid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-aminobutyrate aminotransferase
  • EC number
  • Alternative names
    • GABA aminotransferase (GABA-AT)
    • Gamma-amino-N-butyrate transaminase (GABA transaminase)

Gene names

    • Name
      UGA1
    • Ordered locus names
      YGR019W

Organism names

Accessions

  • Primary accession
    P17649
  • Secondary accessions
    • A5H0J7
    • D6VUF4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001203821-4714-aminobutyrate aminotransferase
Modified residue326N6-(pyridoxal phosphate)lysine

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.

Interaction

Subunit

Homodimer and homotetramer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    52,946
  • Last updated
    1996-10-01 v2
  • Checksum
    33D446778A891F63
MSICEQYYPEEPTKPTVKTESIPGPESQKQLKELGEVFDTRPAYFLADYEKSLGNYITDVDGNTYLDLYAQISSIALGYNNPALIKAAQSPEMIRALVDRPALGNFPSKDLDKILKQILKSAPKGQDHVWSGLSGADANELAFKAAFIYYRAKQRGYDADFSEKENLSVMDNDAPGAPHLAVLSFKRAFHGRLFASGSTTCSKPIHKLDFPAFHWPHAEYPSYQYPLDENSDANRKEDDHCLAIVEELIKTWSIPVAALIIEPIQSEGGDNHASKYFLQKLRDITLKYNVVYIIDEVQTGVGATGKLWCHEYADIQPPVDLVTFSKKFQSAGYFFHDPKFIPNKPYRQFNTWCGEPARMIIAGAIGQEISDKKLTEQCSRVGDYLFKKLEGLQKKYPENFQNLRGKGRGTFIAWDLPTGEKRDLLLKKLKLNGCNVGGCAVHAVRLRPSLTFEEKHADIFIEALAKSVNEL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict240in Ref. 1; CAA36833 and 2; ABF58895

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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