DAAA_LISM4
ID DAAA_LISM4 Reviewed; 289 AA.
AC G2JZ74; O85046;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=LMRG_01347;
OS Listeria monocytogenes serotype 1/2a (strain 10403S).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=393133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=10403S;
RX PubMed=9673233; DOI=10.1128/iai.66.8.3552-3561.1998;
RA Thompson R.J., Bouwer H.G.A., Portnoy D.A., Frankel F.R.;
RT "Pathogenicity and immunogenicity of a Listeria monocytogenes strain that
RT requires D-alanine for growth.";
RL Infect. Immun. 66:3552-3561(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10403S;
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Listeria monocytogenes strain 10403S.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; AF038439; AAC31363.1; -; Genomic_DNA.
DR EMBL; CP002002; AEO06605.1; -; Genomic_DNA.
DR RefSeq; WP_003732538.1; NC_017544.1.
DR AlphaFoldDB; G2JZ74; -.
DR SMR; G2JZ74; -.
DR EnsemblBacteria; AEO06605; AEO06605; LMRG_01347.
DR KEGG; lmt:LMRG_01347; -.
DR HOGENOM; CLU_020844_4_1_9; -.
DR OMA; SMGKMMA; -.
DR Proteomes; UP000001288; 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; 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; Transferase.
FT CHAIN 1..289
FT /note="D-alanine aminotransferase"
FT /id="PRO_0000418518"
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; 32433 MW; 54A14470FE7FEE35 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 ACGELEFAK
