ID   DAAA_STAAR              Reviewed;         282 AA.
AC   Q6GFV1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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; OrderedLocusNames=SAR1835;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40826.1; -; Genomic_DNA.
DR   RefSeq; WP_000411087.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFV1; -.
DR   SMR; Q6GFV1; -.
DR   KEGG; sar:SAR1835; -.
DR   HOGENOM; CLU_020844_4_1_9; -.
DR   OMA; SMGKMMA; -.
DR   OrthoDB; 885013at2; -.
DR   Proteomes; UP000000596; Chromosome.
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..282
FT                   /note="D-alanine aminotransferase"
FT                   /id="PRO_0000103256"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         51
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   BINDING         178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
FT   MOD_RES         146
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19938"
SQ   SEQUENCE   282 AA;  31922 MW;  6B13C32D8EA16A0F CRC64;
     MEKIFLNGEF VSPSEAKVSY NDRGYVFGDG IYEYIRVYNG KLFTVTEHYE RFLRSANEIG
     LDLNYSVEEL IELSRKLVDM NQIETGAIYI QATRGVAERN HSFPTPEVEP AIVAYTKSYD
     RPYDHLENGV NGVTVEDIRW LRCDIKSLNL LGNVLAKEYA VKYNAVEAIQ HRGETVTEGS
     SSNAYAIKDG VIYTHPINNY ILNGITRIVI KKIAEDYNIP FKEETFTVDF LRNADEVIVS
     STSAEVTPVI KLDGEPVNDG KVGPITRQLQ EGFEKYIESH SI