ID DAAA_BACYM Reviewed; 283 AA. AC P19938; P83771; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-SEP-2023, entry version 117. DE RecName: Full=D-alanine aminotransferase; DE EC=2.6.1.21; DE AltName: Full=D-amino acid aminotransferase; DE AltName: Full=D-amino acid transaminase; DE Short=DAAT; DE AltName: Full=D-aspartate aminotransferase; GN Name=dat; OS Bacillus sp. (strain YM-1). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=72579; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2644261; DOI=10.1016/s0021-9258(19)81634-4; RA Tanizawa K., Asano S., Masu Y., Kuramitsu S., Kagamiyama H., Tanaka H., RA Soda K.; RT "The primary structure of thermostable D-amino acid aminotransferase from a RT thermophilic Bacillus species and its correlation with L-amino acid RT aminotransferases."; RL J. Biol. Chem. 264:2450-2454(1989). RN [2] RP PROTEIN SEQUENCE OF 2-21; 143-157 AND 281-283, FUNCTION, CATALYTIC RP ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2914916; DOI=10.1016/s0021-9258(19)81633-2; RA Tanizawa K., Masu Y., Asano S., Tanaka H., Soda K.; RT "Thermostable D-amino acid aminotransferase from a thermophilic Bacillus RT species. Purification, characterization, and active site sequence RT determination."; RL J. Biol. Chem. 264:2445-2449(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), COFACTOR, AND SUBUNIT. RX PubMed=7626635; DOI=10.1021/bi00030a002; RA Sugio S., Petsko G.A., Manning J.M., Soda K., Ringe D.; RT "Crystal structure of a D-amino acid aminotransferase: how the protein RT controls stereoselectivity."; RL Biochemistry 34:9661-9669(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9538014; DOI=10.1021/bi972884d; RA Peisach D., Chipman D.M., van Ophem P.W., Manning J.M., Petsko G.A., RA Ringe D.; RT "Crystallographic study of steps along the reaction pathway of D-amino acid RT aminotransferase."; RL Biochemistry 37:4958-4967(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS OF LEU-202. RX PubMed=9749913; DOI=10.1093/protein/11.8.613; RA Sugio S., Kashima A., Kishimoto K., Peisach D., Petsko G.A., Ringe D., RA Yoshimura T., Esaki N.; RT "Crystal structures of L201A mutant of D-amino acid aminotransferase at RT 2.0-A resolution: implication of the structural role of Leu201 in RT transamination."; RL Protein Eng. 11:613-619(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND MUTAGENESIS OF GLU-178. RX PubMed=9930994; DOI=10.1021/bi982414z; RA van Ophem P.W., Peisach D., Erickson S.D., Soda K., Ringe D., Manning J.M.; RT "Effects of the E177K mutation in D-amino acid transaminase. Studies on an RT essential coenzyme anchoring group that contributes to stereochemical RT fidelity."; RL Biochemistry 38:1323-1331(1999). CC -!- FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate, CC glutamate, aminobutyrate, norvaline and asparagine. The enzyme CC transfers an amino group from a substrate D-amino acid to the pyridoxal CC phosphate cofactor to form pyridoxamine and an alpha-keto acid in the CC first half-reaction. The second-half reaction is the reverse of the CC first, transferring the amino group from the pyridoxamine to a second CC alpha-keto acid to form the product D-amino acid via a ping-pong CC mechanism. This is an important process in the formation of D-alanine CC and D-glutamate, which are essential bacterial cell wall components. CC {ECO:0000269|PubMed:2914916, ECO:0000269|PubMed:9538014}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate; CC Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21; CC Evidence={ECO:0000269|PubMed:2914916, ECO:0000269|PubMed:9538014}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:7626635}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=279 nm {ECO:0000269|PubMed:2914916}; CC Note=Holoenzyme exhibits additional strong peaks at 333 nm and 415 CC nm. Addition of D-alanine causes a decrease in absorbance at 419 nm CC and an increase at 335 nm.; CC Kinetic parameters: CC KM=2.2 mM for D-alanine {ECO:0000269|PubMed:2914916}; CC KM=5.9 mM for alpha-ketoglutarate {ECO:0000269|PubMed:2914916}; CC KM=2.2 mM for alpha-ketobutyrate {ECO:0000269|PubMed:2914916}; CC KM=2.2 mM for alpha-ketovalerate {ECO:0000269|PubMed:2914916}; CC pH dependence: CC Optimum pH is 8.3. {ECO:0000269|PubMed:2914916}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:2914916}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2914916, CC ECO:0000269|PubMed:7626635}. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04460; AAA22252.1; -; Genomic_DNA. DR PIR; A31422; A31422. DR PDB; 1A0G; X-ray; 2.00 A; A/B=2-283. DR PDB; 1DAA; X-ray; 1.94 A; A/B=2-283. DR PDB; 1G2W; X-ray; 2.00 A; A/B=2-283. DR PDB; 2DAA; X-ray; 2.10 A; A/B=2-283. DR PDB; 2DAB; X-ray; 2.00 A; A/B=2-283. DR PDB; 3DAA; X-ray; 1.90 A; A/B=2-278. DR PDB; 3LQS; X-ray; 1.90 A; A/B=2-281. DR PDB; 4DAA; X-ray; 2.40 A; A/B=2-278. DR PDB; 5DAA; X-ray; 2.90 A; A/B=2-278. DR PDBsum; 1A0G; -. DR PDBsum; 1DAA; -. DR PDBsum; 1G2W; -. DR PDBsum; 2DAA; -. DR PDBsum; 2DAB; -. DR PDBsum; 3DAA; -. DR PDBsum; 3LQS; -. DR PDBsum; 4DAA; -. DR PDBsum; 5DAA; -. DR AlphaFoldDB; P19938; -. DR SMR; P19938; -. DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate. DR KEGG; ag:AAA22252; -. DR BRENDA; 2.6.1.21; 691. DR SABIO-RK; P19938; -. DR EvolutionaryTrace; P19938; -. DR GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0046437; P:D-amino acid biosynthetic process; IDA:UniProtKB. DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB. DR CDD; cd01558; D-AAT_like; 1. DR Gene3D; 3.30.470.10; -; 1. DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR018300; Aminotrans_IV_CS. DR InterPro; IPR036038; Aminotransferase-like. DR InterPro; IPR043132; BCAT-like_C. DR InterPro; IPR043131; BCAT-like_N. DR InterPro; IPR005784; D_amino_transT. DR NCBIfam; TIGR01121; D_amino_aminoT; 1. DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1. DR PANTHER; PTHR42743:SF10; D-ALANINE AMINOTRANSFERASE; 1. DR Pfam; PF01063; Aminotran_4; 1. DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Direct protein sequencing; KW Pyridoxal phosphate; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2914916" FT CHAIN 2..283 FT /note="D-alanine aminotransferase" FT /id="PRO_0000103248" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:7626635" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9538014" FT BINDING 51 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:9538014" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9538014" FT BINDING 101 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9538014" FT BINDING 178 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:9538014" FT MOD_RES 146 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000269|PubMed:7626635" FT MUTAGEN 178 FT /note="E->K: Loss of transaminase activity and small gain FT in racemase activity." FT /evidence="ECO:0000269|PubMed:9930994" FT MUTAGEN 202 FT /note="L->A: Inactivates enzyme." FT /evidence="ECO:0000269|PubMed:9749913" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 23..26 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 30..38 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:3LQS" FT HELIX 45..58 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 67..81 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 85..94 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 123..128 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 151..162 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 205..216 FT /evidence="ECO:0007829|PDB:3DAA" FT HELIX 228..232 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:3DAA" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 245..252 FT /evidence="ECO:0007829|PDB:3DAA" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3DAA" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:2DAB" FT HELIX 264..274 FT /evidence="ECO:0007829|PDB:3DAA" SQ SEQUENCE 283 AA; 32396 MW; 21563BDC35BE98F3 CRC64; MGYTLWNDQI VKDEEVKIDK EDRGYQFGDG VYEVVKVYNG EMFTVNEHID RLYASAEKIR ITIPYTKDKF HQLLHELVEK NELNTGHIYF QVTRGTSPRA HQFPENTVKP VIIGYTKENP RPLENLEKGV KATFVEDIRW LRCDIKSLNL LGAVLAKQEA HEKGCYEAIL HRNNTVTEGS SSNVFGIKDG ILYTHPANNM ILKGITRDVV IACANEINMP VKEIPFTTHE ALKMDELFVT STTSEITPVI EIDGKLIRDG KVGEWTRKLQ KQFETKIPKP LHI //