D-alanine aminotransferase

Details

Name
D-alanine aminotransferase
Synonyms
  • 2.6.1.21
  • D-amino acid aminotransferase
  • D-amino acid transaminase
  • D-aspartate aminotransferase
  • DAAT
Gene Name
dat
Organism
Bacillus sp. (strain YM-1)
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
Functions
D-alanine / pyridoxal phosphate binding
Processes
D-amino acid biosynthetic process / D-amino acid catabolic process
General Function
Pyridoxal phosphate binding
Specific 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.
Pfam Domain Function
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
ResourceLink
UniProtKB IDP19938
UniProtKB Entry NameDAAA_BACYM
GenBank Protein ID142542
GenBank Gene IDJ04460
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02142Pyridoxamine-5'-PhosphateexperimentalunknownDetails