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Database: UniProt/TrEMBL
Entry: C9Y2E3_CROTZ
LinkDB: C9Y2E3_CROTZ
Original site: C9Y2E3_CROTZ 
ID   C9Y2E3_CROTZ            Unreviewed;       430 AA.
AC   C9Y2E3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CBA34292.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CBA34292.1};
GN   Name=puuE {ECO:0000313|EMBL:CBA34292.1};
GN   OrderedLocusNames=Ctu_39680 {ECO:0000313|EMBL:CBA34292.1};
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA34292.1, ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RX   PubMed=21037008; DOI=10.1128/JB.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(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       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; FN543093; CBA34292.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9Y2E3; -.
DR   KEGG; ctu:CTU_39680; -.
DR   PATRIC; fig|693216.3.peg.3762; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OMA; VMCGFYA; -.
DR   Proteomes; UP000002069; 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; 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   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:CBA34292.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBA34292.1}.
SQ   SEQUENCE   430 AA;  46207 MW;  37CE051574C38618 CRC64;
     MTFISRRMRV KNSELNQRRQ SATPRGVGVM CGFYAEKADN ATLWDVEGNE IIDFAAGIAV
     LNTGHRHPRV VEAIENQLRA FTHTAYQIVP YESYVSLAER INDCAPIDGP AKTAFFTTGA
     EAVENAVKIA RAYTRRPGLI TFGGGFHGRT FMTMALTGKV APYKIGFGPF PGSVFHAQYP
     NALHGVSVDD AMASLERIFK ADIAPDQVAA IVLEPVQGEG GFNVAPPAFM EALRALCDEH
     GILLIADEVQ SGFARTGKLF AMEHYSVKPD LLTMAKSLAG GMPLSGVVGR AEVMDAPAPG
     GLGGTYAGNP LAVAAAHAVL DVIEQENLCQ RANELGQHLQ EVLNQARTYC PAIAEVRGQG
     SMVAVEFNDP QTGKPSPAFT QDVLTRAREE GLLLLSCGVY GNVIRFLYPL TIPDAQFSKA
     LEILSRALGR
//
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