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B6db families: 2.6.1.40

2.6.1.40
Activity 2.6.1.40
Description (R)-3-amino-2-methylpropionate--pyruvate aminotransferase
Notes The metazoan sequences included in family a are close homologs of alanine:glyoxylate aminotransferase 2 from rat liver; this enzyme appears to be identical to (D)-3-amino-2-methylpropanoate aminotransferase (2.6.1.40) as well as to aminolevulinate aminotransferase (2.6.1.43).

The mammalian enzyme appears to be located exclusively in the mitochondria, in contrast to alanine:glyoxylate aminotransferase 1 which is almost exclusively peroxisomal in herbivores and humans.

In some bacteria (e.g., Streptomyces griseus) similar genes exist, which are part of gene clusters dedicated to pyrimidine degradation. Since (D)-3-amino-2-methylpropanoate is an intermediate of thymine degradation, presumably, these genes encode enzymes with (D)-3-amino-2-methylpropanoate aminotransferase activity. However, such bacterial sequences have not been included in this family.

PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 19
Sequences in seed alignment
MetazoaAGT2_HUMAN (Homo sapiens); XP_001500166 (Equus caballus); XP_969816 (Tribolium castaneum); NP_001028922 (Danio rerio); AAL13781 (Drosophila melanogaster); CAE67402 (Caenorhabditis briggsae); XP_001627014 (Nematostella vectensis); XP_429219 (Gallus gallus); XP_551780 (Anopheles gambiae); NP_491777 (Caenorhabditis elegans); XP_001509172 (Ornithorhynchus anatinus); CAF97143 (Tetraodon nigroviridis); AGT2_RAT (Rattus norvegicus); XP_001373137 (Monodelphis domestica);
ViridiplantaeXP_006429538 (Citrus clementina); AGT23_ARATH (Arabidopsis thaliana); XP_011019036 (Populus euphratica); XP_020971903 (Arachis ipaensis); XP_002531313 (Ricinus communis);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence AGT2_RAT
Domain interval 85-442
Catalytic site 348 K
 
References
 Parthasarathy A, Adams LE, Savka FC, Hudson AO (2019) The Arabidopsis thaliana gene annotated by the locus tag At3g08860 encodes alanine aminotransferase Plant direct 3 e00171.

 Rodionov RN, Murry DJ, Vaulman SF, Stevens JW, Lentz SR. (2010) Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production J Biol Chem 285 5385-91.

 Lee, I. S.; Muragaki, Y.; Ideguchi, T.; Hase, T.; Tsuji, M.; Ooshima, A.; Okuno, E.; Kido, R. (1995) Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney J Biochem (Tokyo) 117 856-62.

 Okuno, E.; Minatogawa, Y.; Kido, R. (1982) Co-purification of alanine-glyoxylate aminotransferase with 2- aminobutyrate aminotransferase in rat kidney Biochim Biophys Acta 715 97-104..

Articles on 2.6.1.40
last changed 2019/09/19 10:11

B6db families