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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//