ID   DAAA_STAES              Reviewed;         282 AA.
AC   Q8CS41;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=SE_1423;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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}.
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; AE015929; AAO05022.1; -; Genomic_DNA.
DR   RefSeq; NP_764978.1; NC_004461.1.
DR   RefSeq; WP_002484981.1; NZ_WBME01000009.1.
DR   AlphaFoldDB; Q8CS41; -.
DR   SMR; Q8CS41; -.
DR   STRING; 176280.SE_1423; -.
DR   EnsemblBacteria; AAO05022; AAO05022; SE_1423.
DR   KEGG; sep:SE_1423; -.
DR   PATRIC; fig|176280.10.peg.1389; -.
DR   eggNOG; COG0115; Bacteria.
DR   HOGENOM; CLU_020844_4_1_9; -.
DR   OMA; SMGKMMA; -.
DR   Proteomes; UP000001411; 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_0000103259"
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;  32163 MW;  8BAB922A757B9F2C CRC64;
     MTKVFINGEF VNEEDAKVSY EDRGYVFGDG IYEYIRAYDG KLFTVKEHFE RFLRSAEEIG
     LDLNYTIEEL IELVRRLLKE NNVVNGGIYI QATRGAAPRN HSFPTPPVKP VIMAFTKSYD
     RPYEELEQGV YAITTEDIRW LRCDIKSLNL LGNVLAKEYA VKYNAAEAIQ HRGDIVTEGA
     SSNVYAIKDG VIYTHPVNNF ILNGITRRVI KWIAEDEQIP FKEEKFTVEF LKSADEVIIS
     STSAEVMPIT KIDGENVQDG QVGTITRQLQ QGFEKYIQSH SI