ID A0A0U4FS90_9BACI Unreviewed; 287 AA.
AC A0A0U4FS90;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-alanine aminotransferase {ECO:0000256|ARBA:ARBA00021779};
DE EC=2.6.1.21 {ECO:0000256|ARBA:ARBA00012874};
DE AltName: Full=D-amino acid aminotransferase {ECO:0000256|ARBA:ARBA00033391};
DE AltName: Full=D-amino acid transaminase {ECO:0000256|ARBA:ARBA00030138};
DE AltName: Full=D-aspartate aminotransferase {ECO:0000256|ARBA:ARBA00033316};
GN ORFNames=AOX59_09080 {ECO:0000313|EMBL:ALX48757.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX48757.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX48757.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX48757.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001188};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR EMBL; CP013862; ALX48757.1; -; Genomic_DNA.
DR RefSeq; WP_068444890.1; NZ_CP013862.1.
DR AlphaFoldDB; A0A0U4FS90; -.
DR STRING; 1472767.AOX59_09080; -.
DR KEGG; lao:AOX59_09080; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000050331; Chromosome.
DR GO; GO:0047810; F:D-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd01558; D-AAT_like; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 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 NCBIfam; TIGR01121; D_amino_aminoT; 1.
DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42743:SF10; D-ALANINE AMINOTRANSFERASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:ALX48757.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050331};
KW Transferase {ECO:0000313|EMBL:ALX48757.1}.
SQ SEQUENCE 287 AA; 32389 MW; 912CA5C97B68FEED CRC64;
MSVYPIILSQ THFTQQEDLT YPFEERGLQF GDGVYEVIRI YDGTYYLLAE HVDRLFRSAE
AIKIVLPFSK KEITDLLLNL LDKNGMDSDG IVYMQATRGS APRTHAFPSE TEANVYAYIR
DMPCKTDDLS KGVSTITERD TRWENCYIKS LNLLPNVLAK QAAQESNSYE AIFHRDGIVT
ECSSSNIFLI KNGNIYTHPA TKRILHGCVR MRIEQFAANL QIPFIEEAFS TADMAMADEL
FLSSTTSEVM PIIEVDNKTI ANGKPGSITR KIQKAYVQDA ALSKVRT
//
