B6db families : 2_6_1_1

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2.6.1.1 b

Activity

2.6.1.1

Description

Aspartate aminotransferase. (family b)

Notes

This family includes enzymes from Archaea and from Gram+ bacteria. The family is strictly related to family 2.6.1.57_b (aromatic amino acid aminotransferase).

PDB

1J32;3HLM;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria	WP_010287371 (Kurthia massiliensis); AAL10665 (Bacillus subtilis); YP_006620675 (Desulfosporosinus meridiei DSM 13257); WP_018885554 (Paenibacillus massiliensis); YP_007212302 (Thermobacillus composti KWC4); WP_019153592 (Bacillus massiliosenegalensis); YP_008968654 (Paenibacillus larvae subsp. larvae DSM 25430); WP_019004326 (Cohnella laeviribosi); WP_019119482 (Brevibacillus massiliensis); WP_017248923 (Brevibacillus brevis);
Archaea	AAT_SULSO (Sulfolobus solfataricus); AAT1_METJA (Methanococcus jannaschii); NP_579431 (Pyrococcus furiosus);
Bacteria	AAO35860 (Clostridium tetani E88); AAT_THEMA (Thermotoga maritima); AAT_RICPR (Rickettsia prowazekii); AAT_AQUAE (Aquifex aeolicus); AAT1_BACSU (Bacillus subtilis); AAT_RHILP (Rhizobium leguminosarum (biovar phaseoli)); BAI68155 (Hydrogenobacter thermophilus TK-6); AAT_STRVG (Streptomyces virginiae); AAT_THETH (Thermus aquaticus (subsp. thermophilus)); AAT_BACSP (Bacillus sp.); AAT_SYNY3 (Synechocystis sp. (strain PCC 6803)); AAT_BACST (Bacillus stearothermophilus); AATA_RHIME (Rhizobium meliloti); AAT_THEAQ (Thermus aquaticus); 1J32A (Phormidium lapideum);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

AAT_THETH

Domain interval

31-378

Catalytic site

234 K

References

Wu HJ, Yang Y, Wang S, Qiao JQ, Xia YF, Wang Y, Wang WD, Gao SF, Liu J, Xue PQ, Gao XW. (2011) Cloning, expression and characterization of a new aspartate aminotransferase from Bacillus subtilis B3 FEBS J. 278 1345-57.

Han Q, Cai T, Tagle DA, Li J. (2010) Structure, expression, and function of kynurenine aminotransferases in human and rodent brains Cell Mol Life Sci. 67 353-68.

Kameya M, Arai H, Ishii M, Igarashi Y. (2010) Purification of three aminotransferases from Hydrogenobacter thermophilus TK-6--novel types of alanine or glycine aminotransferase: enzymes and catalysis FEBS J 277 1876-85.

Ward, D.E.; de Vos, W.M.; van der Oost, J. (2002) Molecular analysis of the role of two aromatic aminotransferases and a broad-specificity aspartate aminotransferase in the aromatic amino acid metabolism of Pyrococcus furiosus Archaea 1 133-41.

O'Farrell, P. A.; Sannia, G.; Walker, J. M.; Doonan, S. (1997) Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1 Biochem Biophys Res Commun 239 810-5.

Bartsch, K.; Schneider, R.; Schulz, A. (1996) Stereospecific production of the herbicide phosphinothricin (glufosinate): purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process Appl Environ Microbiol 62 3794-9.

Okamoto, A.; Kato, R.; Masui, R.; Yamagishi, A.; Oshima, T.; Kuramitsu, S. (1996) An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 J Biochem (Tokyo) 119 135-44.

Articles on 2.6.1.1.b

last changed

2014/03/06 16:24