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Database: UniProt
Entry: A0A3N1I6B2_9ENTR
LinkDB: A0A3N1I6B2_9ENTR
Original site: A0A3N1I6B2_9ENTR 
ID   A0A3N1I6B2_9ENTR        Unreviewed;       289 AA.
AC   A0A3N1I6B2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=D-alanine transaminase {ECO:0000313|EMBL:ROP50067.1};
GN   ORFNames=EDF81_4293 {ECO:0000313|EMBL:ROP50067.1};
OS   Enterobacter sp. BIGb0383.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=2485118 {ECO:0000313|EMBL:ROP50067.1, ECO:0000313|Proteomes:UP000280899};
RN   [1] {ECO:0000313|EMBL:ROP50067.1, ECO:0000313|Proteomes:UP000280899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIGb0383 {ECO:0000313|EMBL:ROP50067.1,
RC   ECO:0000313|Proteomes:UP000280899};
RA   Samuel B.;
RT   "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROP50067.1}.
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DR   EMBL; RJKQ01000005; ROP50067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1I6B2; -.
DR   Proteomes; UP000280899; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
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   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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280899}.
SQ   SEQUENCE   289 AA;  31733 MW;  DB892D10358423A8 CRC64;
     MPRTVYLNGN WLPETQATVS VFDRGFLFAD AVYEVTAVVN GRLVDFAGHY ARLQRSCREL
     QLELPVDKAE LLALHRRLIA DNALLEGGIY LQLTRGSSGD RDFNFPSPTV PPTLLLFTQA
     RAVLNPPQAK SGIRVITCPD IRWQRRDIKT VQLLAPSLAK ALAHAQGADD ALLVEDGYIT
     EGSACNCYLV QGDRTIVTRP LGNTILPGIT RQAILRLAQA QGLTVEERRF TLDEVLQARE
     VFISSATTFV WPVVAVDGQP IGDGTPGPVT QQVREMYLAA LPELSDEAQ
//
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