ID   PUUD_SHISS              Reviewed;         254 AA.
AC   Q3Z146;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase;
DE            Short=Gamma-Glu-GABA hydrolase;
DE            EC=3.5.1.94;
GN   Name=puuD; OrderedLocusNames=SSON_1842;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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=AAZ88516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000038; AAZ88516.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q3Z146; -.
DR   SMR; Q3Z146; -.
DR   MEROPS; C26.961; -.
DR   EnsemblBacteria; AAZ88516; AAZ88516; SSON_1842.
DR   KEGG; ssn:SSON_1842; -.
DR   HOGENOM; CLU_030756_0_0_6; -.
DR   UniPathway; UPA00188; UER00883.
DR   Proteomes; UP000002529; 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.
FT   CHAIN           1..254
FT                   /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase"
FT                   /id="PRO_0000272689"
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;  28013 MW;  ED183250300CCB42 CRC64;
     MENIMNNPVI GVVMCRNRLK GHATQTLQEK YLNAIIHAGG LPIALPHALA EPSLLEQLLP
     KLDGIYLPGS PSNVQPHLYG ENGDEPDADP GRDLLSMAII NAALERRIPI FAICRGLQEL
     VVATGGSLHR KLCEQPELLE HREDPELPVE QQYAPSHEVQ VEEGGLLSAL LPECSNFWVN
     SLHGQGAKVV SPRLRVEARS PDGLVEAVSV INHPFALGVQ WHPEWNSSEY ALSRILFEGF
     ITACQHHIAE KQRL