DAAA_LISMO
ID DAAA_LISMO Reviewed; 289 AA.
AC P0DJL9; O85046;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 44.
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; Synonyms=daaA; OrderedLocusNames=lmo1619;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591980; CAC99697.1; -; Genomic_DNA.
DR PIR; AC1277; AC1277.
DR RefSeq; NP_465144.1; NC_003210.1.
DR RefSeq; WP_009931211.1; NZ_CP023861.1.
DR AlphaFoldDB; P0DJL9; -.
DR SMR; P0DJL9; -.
DR STRING; 169963.lmo1619; -.
DR PaxDb; P0DJL9; -.
DR EnsemblBacteria; CAC99697; CAC99697; CAC99697.
DR GeneID; 985722; -.
DR KEGG; lmo:lmo1619; -.
DR PATRIC; fig|169963.11.peg.1662; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_4_1_9; -.
DR OMA; SMGKMMA; -.
DR PhylomeDB; P0DJL9; -.
DR BioCyc; LMON169963:LMO1619-MON; -.
DR Proteomes; UP000000817; 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:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..289
FT /note="D-alanine aminotransferase"
FT /id="PRO_0000103252"
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 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 147
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 289 AA; 32403 MW; 54A144692E7FEE35 CRC64;
MKVLVNNHLV EREDATVDIE DRGYQFGDGV YEVVRLYNGK FFTYNEHIDR LYASAAKIDL
VIPYSKEELR ELLEKLVAEN NINTGNVYLQ VTRGVQNPRN HVIPDDFPLE GVLTAAAREV
PRNERQFVEG GTAITEEDVR WLRCDIKSLN LLGNILAKNK AHQQNALEAI LHRGEQVTEC
SASNVSIIKD GVLWTHAADN LILNGITRQV IIDVAKKNGI PVKEADFTLT DLREADEVFI
SSTTIEITPI THIDGVQVAD GKRGPITAQL HQYFVEEITR ACGELVFAK
