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B6db families: 2.6.1.44.a

2.6.1.44 a
Activity 2.6.1.44
Description Alanine--glyoxylate aminotransferase. (family a)
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) and aminolevulinate aminotransferase (2.6.1.43).

The mammalian enzyme appears to be located exclusively in the mitochondria, in contrast to isozyme 1 (alanine:glyoxylate aminotransferase 1, enlisted under EC 2.6.1.51) 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.

Three Arabidopsis homologs of rat AGT2 have been described, containing a putative peroxisomal targeting signal (PTS1), but when one of them was expressed in recombinant form, it failed to catalyze the alanine-glyoxylate aminotransferase reaction (See Liepman & Olsen, 2003, Plant Physiol 131 215-27).

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

Number of sequences
14
Sequences in seed alignment
MetazoaXP_969816 (Tribolium castaneum); XP_001373137 (Monodelphis domestica); CAF97143 (Tetraodon nigroviridis); NP_001028922 (Danio rerio); AAL13781 (Drosophila melanogaster); XP_001500166 (Equus caballus); XP_429219 (Gallus gallus); XP_001509172 (Ornithorhynchus anatinus); AGT2_HUMAN (Homo sapiens); NP_491777 (Caenorhabditis elegans); AGT2_RAT (Rattus norvegicus); XP_001627014 (Nematostella vectensis); XP_551780 (Anopheles gambiae); CAE67402 (Caenorhabditis briggsae);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence AGT2_RAT
Domain interval 85-442
Catalytic site 348 K
 
References
 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 2.6.1.44.a
last changed 2011/03/16 12:31

B6db families