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Database: UniProt/TrEMBL
Entry: A0A0P0RA94_9BURK
LinkDB: A0A0P0RA94_9BURK
Original site: A0A0P0RA94_9BURK 
ID   A0A0P0RA94_9BURK        Unreviewed;       415 AA.
AC   A0A0P0RA94;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=K788_0002580 {ECO:0000313|EMBL:ALL65080.1};
OS   Paraburkholderia caribensis MBA4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1323664 {ECO:0000313|EMBL:ALL65080.1, ECO:0000313|Proteomes:UP000019146};
RN   [1] {ECO:0000313|EMBL:ALL65080.1, ECO:0000313|Proteomes:UP000019146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBA4 {ECO:0000313|EMBL:ALL65080.1,
RC   ECO:0000313|Proteomes:UP000019146};
RX   PubMed=24558235;
RA   Pan Y., Kong K.F., Tsang J.S.;
RT   "Draft Genome Sequence of the Haloacid-Degrading Burkholderia caribensis
RT   Strain MBA4.";
RL   Genome Announc. 2:e00047-e00014(2014).
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; CP012746; ALL65080.1; -; Genomic_DNA.
DR   RefSeq; WP_035539403.1; NZ_CP012746.1.
DR   AlphaFoldDB; A0A0P0RA94; -.
DR   GeneID; 69969170; -.
DR   KEGG; bcai:K788_0002580; -.
DR   Proteomes; UP000019146; Chromosome 1.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC.
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:ALL65080.1};
KW   Transferase {ECO:0000313|EMBL:ALL65080.1}.
FT   DOMAIN          38..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   415 AA;  46068 MW;  AE70746946303738 CRC64;
     MPVVKPILKS NKLLNVCYDI RGPVLEHAKR LEEEGHRIIK LNIGNLAPFG FEAPDEIIQD
     MIRNLPTSSG YSDSKGVFAA RKAIMHYAQQ KGVVGVELDD IYIGNGASEL IVMALQALLN
     DGDEVLLPAP DYPLWTAGVS LSGGTPVHYI CDESNAWMPD LDDIRAKITP NTKALVVINP
     NNPTGALYSD ELLLGLIAIA REHGLVIFAD EVYDKIIYDG KTHTSMASLS EDVLTVTFNS
     LSKSYRSCGY RAGWMWVSGL TGENRRRAKD YFEGLGILAS MRLCPNVPGQ YAIQTALGGY
     QSINELIAPG GRLYKQRELA YDMLTAIPGV TCVKPEAALY MFPRLDPKLY PIENDQQFIL
     DLLLEERVLL VQGSGFNWKT PDHFRVVFLP NVDDLADSIH RIARFLDGYR KRHAA
//
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