ID   D2AHK8_SHIF2            Unreviewed;       375 AA.
AC   D2AHK8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ADA75021.1};
GN   Name=gabT {ECO:0000313|EMBL:ADA75021.1};
GN   OrderedLocusNames=SFxv_2948 {ECO:0000313|EMBL:ADA75021.1};
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA75021.1, ECO:0000313|Proteomes:UP000001884};
RN   [1] {ECO:0000313|EMBL:ADA75021.1, ECO:0000313|Proteomes:UP000001884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017 {ECO:0000313|EMBL:ADA75021.1,
RC   ECO:0000313|Proteomes:UP000001884};
RX   PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
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|RuleBase:RU003560}.
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DR   EMBL; CP001383; ADA75021.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2AHK8; -.
DR   SMR; D2AHK8; -.
DR   KEGG; sfe:SFxv_2948; -.
DR   PATRIC; fig|591020.3.peg.3198; -.
DR   HOGENOM; CLU_016922_10_2_6; -.
DR   Proteomes; UP000001884; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ADA75021.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ADA75021.1}.
SQ   SEQUENCE   375 AA;  40054 MW;  EB4C01006704BBBA CRC64;
     MLNTGHLHPK VVAAVEAQLK KLSHTCFQVL AYEPYLELCE IMNQKVPGDF AKKTLLVTTG
     SEAVENAVKI ARAATKRSGT IAFSGEYHGR THYTLALTGK VNPYSAGMGL MPGHVYRALY
     PCPLHGISED DAIASIHRIF KNDAAPEDIA AIMIEPVQGE GGFYAASPAF MQRLRALCDE
     HGIMLIADEV QSGAGRTGTL FAMEQMGVAP DLTTFAKSIA GGFPLAGVTG RAEVMDAVAP
     GGLGGTYAGN PIACVAALEV LKVFEQENLL QKANDLGQKL KDGLLAIAEK HPEIGDVRGL
     GSMIAIELFE DGDHSKPDAK LTAEIVARAR DKGLILLSCG PYYNVLRILV PLTIEDAQIR
     QGLEIIGQCF DEAKQ
//