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Database: UniProt/TrEMBL
Entry: A0A132ERU7_9BURK
LinkDB: A0A132ERU7_9BURK
Original site: A0A132ERU7_9BURK 
ID   A0A132ERU7_9BURK        Unreviewed;       412 AA.
AC   A0A132ERU7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=WT57_31610 {ECO:0000313|EMBL:KWF56703.1};
OS   Burkholderia pseudomultivorans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=1207504 {ECO:0000313|EMBL:KWF56703.1, ECO:0000313|Proteomes:UP000061512};
RN   [1] {ECO:0000313|EMBL:KWF56703.1, ECO:0000313|Proteomes:UP000061512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSMB574WGS {ECO:0000313|EMBL:KWF56703.1,
RC   ECO:0000313|Proteomes:UP000061512};
RA   Sahl J., Keim P., Wagner D.;
RT   "Expanding the genomic diversity of Burkholderia species for the
RT   development of highly accurate diagnostics.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KWF56703.1}.
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DR   EMBL; LPJX01000071; KWF56703.1; -; Genomic_DNA.
DR   RefSeq; WP_009694053.1; NZ_LPLB01000047.1.
DR   AlphaFoldDB; A0A132ERU7; -.
DR   KEGG; bpsl:WS57_27590; -.
DR   Proteomes; UP000061512; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KWF56703.1};
KW   Transferase {ECO:0000313|EMBL:KWF56703.1}.
FT   DOMAIN          35..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   412 AA;  45741 MW;  61574A91D8B9821C CRC64;
     MKPIQKSNKL LNVCYDIRGP VLEHAKRLEE EGHRIIKLNI GNLAPFGFDA PDEIIQDMIR
     NLPTSSGYSD SKGVFSARKA VMHYTQQKGV VGVGLDDIYI GNGASELIVM ATQALLNDGD
     EVLLPAPDYP LWTAAVSLSG GTPVHYICDE QNAWMPDLDD IRRKITPNTK AIVVINPNNP
     TGALYSDALL LELLEIARQH GLIVFADEVY DKIVYDGLEH TAMGALSEDV ITVTFNSLSK
     SYRSCGYRAG WMAVSGLGGD NRRRAKDYLE GLGILSSMRL CANVPGQFAI QTALGGYQSI
     NELIVPSGRL FKQRELAYDM LTSIPGVTCV KPQAALYMFP RLDPKLYPIQ NDQQFILDLL
     LEERVLLVQG TGFNWPTPDH FRVVFLPNLE DLADSIERIA RFLDGYRKRH TA
//
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