ID   PUUD_ECO57              Reviewed;         254 AA.
AC   Q8X7G2; Q7AEJ1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase;
DE            Short=Gamma-Glu-GABA hydrolase;
DE            EC=3.5.1.94;
GN   Name=puuD; OrderedLocusNames=Z2490, ECs1875;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in the breakdown of putrescine via hydrolysis of the
CC       gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(gamma-L-glutamylamino)butanoate + H2O = 4-aminobutanoate +
CC         L-glutamate; Xref=Rhea:RHEA:19737, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58800, ChEBI:CHEBI:59888; EC=3.5.1.94;
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC       aminobutanoate from putrescine: step 4/4.
CC   -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG56506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB35298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG56506.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB35298.1; ALT_INIT; Genomic_DNA.
DR   PIR; C90863; C90863.
DR   PIR; F85755; F85755.
DR   RefSeq; NP_309902.2; NC_002695.1.
DR   RefSeq; WP_001322278.1; NZ_SEKU01000010.1.
DR   AlphaFoldDB; Q8X7G2; -.
DR   SMR; Q8X7G2; -.
DR   STRING; 155864.EDL933_2385; -.
DR   MEROPS; C26.961; -.
DR   EnsemblBacteria; AAG56506; AAG56506; Z2490.
DR   EnsemblBacteria; BAB35298; BAB35298; ECs_1875.
DR   GeneID; 912701; -.
DR   KEGG; ece:Z2490; -.
DR   KEGG; ecs:ECs_1875; -.
DR   PATRIC; fig|386585.9.peg.1978; -.
DR   eggNOG; COG2071; Bacteria.
DR   HOGENOM; CLU_030756_0_0_6; -.
DR   OMA; PTYHHQA; -.
DR   UniPathway; UPA00188; UER00883.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0033969; F:gamma-glutamyl-gamma-aminobutyrate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR011697; Peptidase_C26.
DR   InterPro; IPR044668; PuuD-like.
DR   PANTHER; PTHR43235; PTHR43235; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase; Hydrolase; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase"
FT                   /id="PRO_0000272687"
FT   DOMAIN          16..250
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   254 AA;  28085 MW;  B71D97A9C990F722 CRC64;
     MENIMNNPVI GVVMCRNRLK GHATQTLQEK YLNAIIHAGG LPIALPHALA EPSLLEQLLP
     KLDGIYLPGS PSNVQPHLYG ENGDEPDADP ERDLLSMALI NAALERRIPI FAICRGLQEL
     VVATGGSLHR KLCEQPELLE HREDPELPVE QQYAPSHEVQ VEEGGLLSAL LPECSNFWVN
     SLHGQGAKVV SPRLRVEARS PDGLVEAVSV INHPFALGVQ WHPEWNSSEY ALSRILFEGF
     ITACQHHIAE KQRL