ID   A7ZLD0_ECO24            Unreviewed;       421 AA.
AC   A7ZLD0;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ABV18436.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABV18436.1};
GN   Name=gabT1 {ECO:0000313|EMBL:ABV18436.1};
GN   OrderedLocusNames=EcE24377A_1512 {ECO:0000313|EMBL:ABV18436.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV18436.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000800; ABV18436.1; -; Genomic_DNA.
DR   RefSeq; WP_000069229.1; NC_009801.1.
DR   AlphaFoldDB; A7ZLD0; -.
DR   SMR; A7ZLD0; -.
DR   KEGG; ecw:EcE24377A_1512; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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; IPR004632; 4NH2But_aminotransferase_bac.
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   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:ABV18436.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW   Transferase {ECO:0000313|EMBL:ABV18436.1}.
SQ   SEQUENCE   421 AA;  44729 MW;  A2C17A885FEBE4EB CRC64;
     MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA VLNTGHRHPD
     LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG QAKTAFFTTG AEAVENAVKI
     ARAHTGRPGV IAFSGGFHGR TYMTMALTGK VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ
     DSLDAIERLF KSDIEAKQVA AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV
     QSGFARTGKL FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN
     PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL GSMIAVEFND
     PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP LTIPDAQFDA AMKILQDALS
     D
//