ID A0A0U1P2H0_9BACI Unreviewed; 290 AA.
AC A0A0U1P2H0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=D-alanine aminotransferase {ECO:0000256|ARBA:ARBA00021779, ECO:0000256|RuleBase:RU004520};
DE EC=2.6.1.21 {ECO:0000256|ARBA:ARBA00012874, ECO:0000256|RuleBase:RU004520};
GN ORFNames=BN000_04468 {ECO:0000313|EMBL:CRK84455.1};
OS Neobacillus massiliamazoniensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK84455.1, ECO:0000313|Proteomes:UP000199087};
RN [1] {ECO:0000313|Proteomes:UP000199087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LF1 {ECO:0000313|Proteomes:UP000199087};
RA Urmite Genomes;
RL Submitted (MAY-2015) 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. {ECO:0000256|RuleBase:RU004520}.
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 ECO:0000256|RuleBase:RU004520};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004516};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC ECO:0000256|RuleBase:RU004106}.
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DR EMBL; CVRB01000004; CRK84455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1P2H0; -.
DR STRING; 1499688.BN000_04468; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000199087; Unassembled WGS sequence.
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; 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 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.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CRK84455.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000199087};
KW Transferase {ECO:0000313|EMBL:CRK84455.1}.
SQ SEQUENCE 290 AA; 32744 MW; D8098B13B20F5D55 CRC64;
MEFAILHGEI VKRSEAKVDV EDRGYQFGDG VYEVIRVYNG KMFTEHEHLN RLAKSTDSIG
ISLPFTNENL KGLLVELIEK NKLQNGIIYM QVTRGVALRN HAFPTEYVTP CLTTYTKKIE
RPVDSMRSGV KTILTEDIRW LRCDIKSLNL LGNVLAKQKA AEAGCFEVIQ HRGQEVTEGS
TSNIFIVKND IVITHASDHL ILKGITKDVL LVVCAKNNLR VEERMFTIEE LKQADECFLT
SSTSEVMPIV EIDGNKISNG IPGPITRKLQ EWFGQEIEKQ CGSLNEKITF
//
