ID R4WVV5_9BURK Unreviewed; 412 AA.
AC R4WVV5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=BRPE64_ACDS13270 {ECO:0000313|EMBL:BAN23081.1};
OS Caballeronia insecticola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN23081.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN23081.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN23081.1};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
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; AP013058; BAN23081.1; -; Genomic_DNA.
DR RefSeq; WP_016345235.1; NC_021287.1.
DR AlphaFoldDB; R4WVV5; -.
DR STRING; 758793.BRPE64_ACDS13270; -.
DR KEGG; buo:BRPE64_ACDS13270; -.
DR PATRIC; fig|758793.3.peg.1329; -.
DR HOGENOM; CLU_017584_4_2_4; -.
DR Proteomes; UP000013966; 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:BAN23081.1};
KW Transferase {ECO:0000313|EMBL:BAN23081.1}.
FT DOMAIN 35..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 412 AA; 45934 MW; 5222413B40C03B47 CRC64;
MKPILKSNKL QNVCYDIRGP VLEHAKRLEE EGHRIIKLNI GNLAPFGFEA PDEIIQDMIR
NLPGSSGYSD SKGVFAARKA IMHYTQQKGV TGVELDDIYI GNGASELIVM AMQALLNDGD
EVLLPAPDYP LWTAAVSLSS GTPRHYMCDE SNGWMPDLDD IRAKITPNTK ALVVINPNNP
TGALYSDELL LDLISIAREH GLIIFADEVY DKIIYDGMTH TSMAALSEDV ITVTFNSLSK
SYRSCGYRAG WMAISGLIEE NRRRAKDYLE GLGILASMRL CPNVPGQYAI QTALGGYQSI
NDLILPGGRL FKQRELAYDM LTAIPGVSCV KPQAALYMFP KLDPKMYPIQ DDQQFITDLL
LEERVLLVQG TGFNWPTPDH FRVVFLPNVD DLADSINRIA RFLDGYRKRH FA
//
