A0A218UWT1 · A0A218UWT1_9PASE

Function

function

Multifunctional aminotransferase with a broad substrate specifcity. Catalyzes the conversion of glyoxylate to glycine using alanine as the amino donor. Catalyzes metabolism of not L- but the D-isomer of D-beta-aminoisobutyric acid to generate 2-methyl-3-oxopropanoate and alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. Can metabolize NG-monomethyl-L-arginine (NMMA), asymmetric NG,NG-dimethyl-L-arginine (ADMA) and symmetric NG,N'G-dimethyl-L-arginine (SDMA). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • (2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine
  • (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine
    This reaction proceeds in the forward direction.
    EC:2.6.1.40 (UniProtKB | ENZYME | Rhea)
  • 2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate
    EC:2.6.1.44 (UniProtKB | ENZYME | Rhea)
  • 2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = L-2-aminohexanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate
  • 2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate
  • 3-oxopropanoate + L-alanine = beta-alanine + pyruvate
    This reaction proceeds in the backward direction.
    EC:2.6.1.18 (UniProtKB | ENZYME | Rhea)
  • L-ornithine + glyoxylate = 5-amino-2-oxopentanoate + glycine
  • L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine
  • N(omega),N('omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + glycine
  • N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + L-alanine
  • N(omega),N(omega)-dimethyl-L-arginine + 2-oxobutanoate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + (2S)-2-aminobutanoate
  • N(omega),N(omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + glycine
  • N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-aspartate
  • N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-alanine
  • N(omega)-methyl-L-arginine + glyoxylate = 5-(3-methylguanidino)-2-oxopentanoate + glycine
  • N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)-2-oxopentanoate + L-alanine
  • glyoxylate + L-alanine = glycine + pyruvate
    This reaction proceeds in the forward direction.
    EC:2.6.1.44 (UniProtKB | ENZYME | Rhea)
  • oxaloacetate + L-alanine = L-aspartate + pyruvate

Cofactor

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

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Functionalanine-glyoxylate transaminase activity
Molecular Functionpyridoxal phosphate binding
Biological Processglyoxylate catabolic process
Biological ProcessL-alanine catabolic process, by transamination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alanine--glyoxylate aminotransferase 2, mitochondrial
  • EC number
  • Alternative names
    • (R)-3-amino-2-methylpropionate--pyruvate transaminase
    • Beta-ALAAT II
    • Beta-alanine-pyruvate aminotransferase
    • D-3-aminoisobutyrate-pyruvate aminotransferase
    • D-AIBAT
    • D-beta-aminoisobutyrate-pyruvate aminotransferase

Gene names

    • Name
      AGXT2
    • ORF names
      RLOC_00010824

Organism names

  • Taxonomic identifier
  • Strain
    • White83orange57
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Estrildidae > Estrildinae > Lonchura

Accessions

  • Primary accession
    A0A218UWT1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-10Basic and acidic residues
Region1-34Disordered

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    426
  • Mass (Da)
    47,775
  • Last updated
    2017-09-27 v1
  • MD5 Checksum
    2B034447E4B4D2C34ACA20BA1521156E
MTSREWHAKAPEGQQHTRRGGAEPGRRRWRRGGSAASYPYERMQKIREQNIAPSLRTYYKKPLLLHQGHMQWLFDHEGQRYLDLFAGIVTVSVGHCHPKVTMATQKQLARLWHTTNIYMYPAIHEYAEKLTSLFPDPLKVVYLTNSGSEANDLAMFMARLHTRNFDIISLRQCYQMFFVVHGEAAIVEILQCKLFENAAALKGVNGAVQYPRNFLKEAYQLIREKGGLCISDEVQTGFGRTGSHFWGFQTHGVVPDIVTLAKGIGNGFPMAAVVTTKEIASSLAQNLHFNTFGGNPLACVVGAAVLDAIEEDGLQKNSEDVGTYMLLELAKLRDKFEIVGDVRGKGLMIGVEMVTDKDNRHPLPAEEISQIWEDCKDMGVLIGRGGLYSQTFRIKPPMCITKSDVDFAVEVFCTALQRHVERAAAK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-10Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MUZQ01000116
EMBL· GenBank· DDBJ
OWK57792.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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