ID   B0RNZ1_XANCB            Unreviewed;       423 AA.
AC   B0RNZ1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=XCCB100_0833 {ECO:0000313|EMBL:CAP50176.1};
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP50176.1, ECO:0000313|Proteomes:UP000001188};
RN   [1] {ECO:0000313|EMBL:CAP50176.1, ECO:0000313|Proteomes:UP000001188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100 {ECO:0000313|EMBL:CAP50176.1,
RC   ECO:0000313|Proteomes:UP000001188};
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA   Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA   Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50176.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RNZ1; -.
DR   KEGG; xca:xcc-b100_0833; -.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000001188; Chromosome.
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:CAP50176.1};
KW   Transferase {ECO:0000313|EMBL:CAP50176.1}.
FT   DOMAIN          39..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   423 AA;  46139 MW;  5D697F62263DB996 CRC64;
     MSTAPQKPLA IRERLSEVRY EIRGELARRA RELEAQGRKL IKLNIGNPGA FGFRAPEHLQ
     RAIADDMGRT DPYTHQQGLP EAREAIAAAY ARRQHPDAHP DRIFIGNGVS ELIDLSLRAL
     LNPGDEVLVP SPDYPLWSAA TILNDGRPVY YRCAPENGFQ PDPVEIETLV SSRTRAIVLI
     NPNNPSGASY SRELLERIVA IAVKHNLLLM VDEIYDQVLY DGAAFVPVAP LAGEHPCITF
     SGLSKVHRAC GWRVGWALLS GEQSRINDLR NAMDLLGALR LCANVPGQYA IDAAVNGPDT
     ISALCAPGGR LYETRRAVIE ACAASSHLSL VAPAGALYAF PAVVGPAARA FDDHTFALDL
     MNDEGVLVVP GSSFNVPYRH HFRVTLMPEA AVMRDVFARI DRALTRRAEA VTKVVPLKSR
     SVA
//