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Database: UniProt
Entry: F0C3E6_9XANT
LinkDB: F0C3E6_9XANT
Original site: F0C3E6_9XANT 
ID   F0C3E6_9XANT            Unreviewed;       240 AA.
AC   F0C3E6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:EGD19946.1};
GN   ORFNames=XGA_1392 {ECO:0000313|EMBL:EGD19946.1};
OS   Xanthomonas hortorum ATCC 19865.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX   NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD19946.1, ECO:0000313|Proteomes:UP000005023};
RN   [1] {ECO:0000313|EMBL:EGD19946.1, ECO:0000313|Proteomes:UP000005023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD19946.1,
RC   ECO:0000313|Proteomes:UP000005023};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGD19946.1}.
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DR   EMBL; AEQX01000137; EGD19946.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0C3E6; -.
DR   PATRIC; fig|925777.8.peg.4289; -.
DR   Proteomes; UP000005023; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EGD19946.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:EGD19946.1}.
SQ   SEQUENCE   240 AA;  25958 MW;  F9BA2FB8DF8C7A16 CRC64;
     MEPAMHDHPL SDQAHALQAP SQLDAFWMPF TANRQFKARP RLLASAAGMY YRDVDGRQIL
     DGAAGLWCCN AGHGRARIVA AIRAQAGTLD FAPTFQMGSP LPFVLAQRLA AIAPPGLGHV
     FFTNSGSEAV DSAMKIVLAY HRLRGEGQRT RFIGREKAYH GVGFGGMSIG GLPNNRKWFG
     PLLAGTDHLR HTLDIERNAY SRGLPAHGAE LADDLERLIT LHDASTIAAV FVEPVSARPA
//
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