P0A959 · ALAA_ECOLI

Function

function

Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction.

Catalytic activity

Cofactor

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.55 mMpyruvate8.537
4.9 mMalanine8.537

Pathway

Amino-acid biosynthesis; L-alanine biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site41L-alanine (UniProtKB | ChEBI)
Binding site179L-alanine (UniProtKB | ChEBI)
Binding site378L-alanine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionL-alanine:2-oxoglutarate aminotransferase activity
Molecular Functionprotein homodimerization activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
Biological Processalanine biosynthetic process
Biological ProcessD-alanine biosynthetic process
Biological ProcessDNA damage response
Biological ProcessL-alanine biosynthetic process from pyruvate
Biological Processresponse to antibiotic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate-pyruvate aminotransferase AlaA
  • EC number

Gene names

    • Name
      alaA
    • Synonyms
      yfbQ
    • Ordered locus names
      b2290, JW2287

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0A959
  • Secondary accessions
    • P77727

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001238661-405Glutamate-pyruvate aminotransferase AlaA
Modified residue240N6-(pyridoxal phosphate)lysine

Proteomic databases

Expression

Induction

Modestly repressed by alanine and leucine via Lrp.

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    405
  • Mass (Da)
    45,517
  • Last updated
    2005-07-19 v1
  • Checksum
    6A5E78876CC3C388
MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFITPGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKMVLDFLLQEKVLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSGYHQL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00096
EMBL· GenBank· DDBJ
AAC75350.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16127.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp