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;1O4S;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Archaea

AAB89121 (Archaeoglobus fulgidus DSM 4304); WP_012966888 (Ferroglobus placidus); AAT1_METJA (Methanococcus jannaschii); WP_048088009 (Metallosphaera yellowstonensis); AAT_SULSO (Sulfolobus solfataricus); WP_013603386 (Vulcanisaeta moutnovskia); WP_013683744 (Archaeoglobus veneficus); NP_579431 (Pyrococcus furiosus);

Bacteria

AAT_BACSP (Bacillus sp.); AAT_THEMA (Thermotoga maritima); AAT_THETH (Thermus aquaticus subsp. thermophilus); AAT_STRVG (Streptomyces virginiae); AAT1_BACSU (Bacillus subtilis); AAM24590 (Caldanaerobacter subterraneus subsp. tengcongensis MB4); BAB76552 (Nostoc sp. PCC 7120); AAT_SYNY3 (Synechocystis sp. strain PCC 6803); BAI68155 (Hydrogenobacter thermophilus TK-6); WP_033191801 (Fervidobacterium islandicum); AAT_BACST (Bacillus stearothermophilus); AAT_AQUAE (Aquifex aeolicus); AAT_RICPR (Rickettsia prowazekii); AAM24436 (Caldanaerobacter subterraneus subsp. tengcongensis MB4); AAT_THEAQ (Thermus aquaticus); AATA_RHIME (Rhizobium meliloti); WP_010580007 (Lactobacillus vini); AHN09463 (Lactobacillus brevis); AAT_RHILP (Rhizobium leguminosarum (biovar phaseoli)); 1J32A (Phormidium lapideum); WP_002771821 (Leptonema illini); AAO35860 (Clostridium tetani E88);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

AAT_THETH

Domain interval

31-378

Catalytic site

234 K

References

Sheng Hu S, Zhang X, Lu Y, Lin Y-C, Xie D-F, Fang H, Huang J, Mei L-H (2017) Cloning, expression and characterization of an aspartate aminotransferase gene from Lactobacillus brevis CGMCC 1306 Biotechnology & Biotechnological Equipment 31 1219-30.

Xu X, Gu L, He P, Zhou R (2015) Characterization of five putative aspartate aminotransferase genes in the N2-fixing heterocystous cyanobacterium Anabaena sp. strain PCC 7120 Microbiology 161 1219-30.

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.

Koma D, Sawai T, Hara R, Harayama S, Kino K. (2008) Two groups of thermophilic amino acid aminotransferases exhibiting broad substrate specificities for the synthesis of phenylglycine derivatives Appl Microbiol Biotechnol 79 775-84.

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.

Marino, G.; Nitti, G.; Arnone, M. I.; Sannia, G.; Gambacorta, A.; De Rosa, M. (1988) Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus J Biol Chem 263 12305-9.

Articles on 2.6.1.1.b

last changed

2018/10/15 13:19