D-alanine aminotransferase
Details
- Name
- D-alanine aminotransferase
- Kind
- protein
- Synonyms
- 2.6.1.21
- D-amino acid aminotransferase
- D-amino acid transaminase
- D-aspartate aminotransferase
- DAAT
- Gene Name
- dat
- UniProtKB Entry
- P19938Swiss-Prot
- Organism
- Bacillus sp. (strain YM-1)
- NCBI Taxonomy ID
- 72579
- Amino acid sequence
>lcl|BSEQ0011065|D-alanine aminotransferase MGYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDRLYASAEKIR ITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENP RPLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAHEKGCYEAILHRNNTVTEGS SSNVFGIKDGILYTHPANNMILKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVT STTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIPKPLHI
- Number of residues
- 283
- Molecular Weight
- 32395.92
- Theoretical pI
- 6.68
- GO Classification
- FunctionsD-alanine / pyridoxal phosphate bindingProcessesD-amino acid biosynthetic process / D-amino acid catabolic process
- General Function
- Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.
- Specific Function
- D-alanine
- Pfam Domain Function
- Aminotran_4 (PF01063)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0002995|852 bp ATGGGATACACTTTATGGAATGACCAAATCGTGAAAGATGAAGAAGTCAAAATTGATAAA GAAGATCGCGGTTATCAATTCGGTGATGGCGTATATGAAGTTGTGAAAGTATATAACGGT GAAATGTTTACTGTAAATGAACATATTGACCGATTATATGCATCAGCTGAAAAAATACGA ATTACGATTCCATATACAAAGGATAAATTTCATCAATTGCTACATGAATTAGTGGAAAAA AATGAATTAAACACTGGGCATATTTATTTTCAAGTTACTCGCGGAACTTCGCCTCGTGCG CATCAATTCCCTGAGAATACTGTAAAACCAGTAATCATCGGTTATACGAAAGAAAATCCA CGACCATTAGAAAATCTTGAAAAAGGTGTAAAAGCTACCTTTGTGGAAGATATCCGTTGG TTACGATGTGATATTAAATCTTTGAACTTGCTTGGTGCAGTATTAGCAAAACAAGAAGCT CATGAAAAAGGCTGCTATGAAGCGATTCTACATCGAAATAATACAGTAACAGAAGGCTCT TCTTCAAATGTATTTGGAATAAAAGATGGTATATTGTATACCCATCCTGCAAACAATATG ATTTTAAAAGGAATCACTCGCGACGTTGTCATAGCTTGTGCAAATGAAATTAATATGCCT GTAAAAGAAATTCCATTTACAACTCATGAAGCATTGAAAATGGATGAATTATTTGTAACA AGTACAACTTCTGAAATTACGCCGGTTATTGAAATAGATGGTAAGTTGATTCGAGATGGA AAAGTTGGAGAATGGACTCGTAAATTACAAAAACAATTTGAAACAAAAATTCCAAAACCG CTTCATATATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P19938 UniProtKB Entry Name DAAA_BACYM GenBank Protein ID 142542 GenBank Gene ID J04460 PDB ID(s) 1A0G, 1DAA, 1G2W, 2DAA, 2DAB, 3DAA, 3LQS, 4DAA, 5DAA - General References
- Tanizawa K, Asano S, Masu Y, Kuramitsu S, Kagamiyama H, Tanaka H, Soda K: The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases. J Biol Chem. 1989 Feb 15;264(5):2450-4. [Article]
- Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K: Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination. J Biol Chem. 1989 Feb 15;264(5):2445-9. [Article]
- Sugio S, Petsko GA, Manning JM, Soda K, Ringe D: Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry. 1995 Aug 1;34(30):9661-9. [Article]
- Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D: Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. Biochemistry. 1998 Apr 7;37(14):4958-67. [Article]
- Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N: Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. Protein Eng. 1998 Aug;11(8):613-9. [Article]
- van Ophem PW, Peisach D, Erickson SD, Soda K, Ringe D, Manning JM: Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity. Biochemistry. 1999 Jan 26;38(4):1323-31. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Pyridoxamine-5'-Phosphate experimental unknown target Details