DAAA_BACYM
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 03-AUG-2022, entry version 113.
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; Firmicutes; 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}.
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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 Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 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 Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01121; D_amino_aminoT; 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
