ID   DAAA_BACLI              Reviewed;         283 AA.
AC   P54692;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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 licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10716 / DSM 603 / NBRC 12199 / NCIMB 8874 / Tracy I;
RX   PubMed=9003455; DOI=10.1016/s0167-4781(96)00204-7;
RA   Taylor P.P., Fotheringham I.G.;
RT   "Nucleotide sequence of the Bacillus licheniformis ATCC 10716 dat gene and
RT   comparison of the predicted amino acid sequence with those of other
RT   bacterial species.";
RL   Biochim. Biophys. Acta 1350:38-40(1997).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U26947; AAB50428.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54692; -.
DR   SMR; P54692; -.
DR   PATRIC; fig|1402.64.peg.1229; -.
DR   GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0046437; P:D-amino acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019478; P:D-amino acid catabolic process; ISS: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   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..283
FT                   /note="D-alanine aminotransferase"
FT                   /id="PRO_0000103246"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         50
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         176
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   MOD_RES         144
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
SQ   SEQUENCE   283 AA;  31396 MW;  2CA8FA604FEDE9D7 CRC64;
     MKVLFNGRLM ERSECAVDIE DRGYQFGDGV YEVIRIYNGI LFTLDEHIAR LYKSAAEIGI
     DLSFSEAELK SQLKELVDIN QRRDGGLYLQ VTRGKAPRKH QYGAGLTPQV TAYTFPIQKP
     EKEQQNGVSA ITADDMRWLR CDIKSLNLLY NVMIKQKAQE ASAFEAILIR DGLVTEGTSS
     NVYVAKQNVI YTHPVTTLIL NGITRMKVLQ LCEENGLNYE EKAVTKDELL NADEVFITST
     TAEVIPVTSI DGQTIGSGAP GPLTKNVQTA LQNSILSETA KTV