ID   Q0BES4_BURCM            Unreviewed;       412 AA.
AC   Q0BES4;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Bamb_1793 {ECO:0000313|EMBL:ABI87349.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI87349.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000440; ABI87349.1; -; Genomic_DNA.
DR   RefSeq; WP_011657054.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BES4; -.
DR   GeneID; 69544040; -.
DR   KEGG; bam:Bamb_1793; -.
DR   PATRIC; fig|339670.21.peg.3167; -.
DR   eggNOG; COG0436; Bacteria.
DR   Proteomes; UP000000662; Chromosome 1.
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:ABI87349.1};
KW   Transferase {ECO:0000313|EMBL:ABI87349.1}.
FT   DOMAIN          35..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   412 AA;  45671 MW;  7E11FD55EDF75060 CRC64;
     MKPIQKSNKL LNVCYDIRGP VLEHAKRLEE EGHRIIKLNI GNLAPFGFDA PDEIIQDMIR
     NLPASSGYSD SKGVFSARKA VMHYTQQKGV VGVGLDDIYI GNGASELIVM ATQALLNDGD
     EVLLPAPDYP LWTAAVSLSG GTPVHYVCDE QNAWMPDLDD IRRKITPNTK AIVVINPNNP
     TGALYSDELL LELLAIAREH GLIVFADEVY DKIVYDGLEH TALGSLSEDV ITVTFNSLSK
     SYRSCGYRAG WMAVSGLGGD NRRRAKDYLE GLGILSSMRL CANVPGQFAI QTALGGYQSI
     NELIVPSGRL YKQRELAYDM LTSIPGVTCV KPQAALYMFP RLDPKLYPIQ NDQQFILDLL
     LEERVLLVQG TGFNWAAPDH FRVVFLPNLD DLTDSINRIA RFLDGYRKRH SV
//