ID   PUUD_SHIFL              Reviewed;         254 AA.
AC   Q83LB6; Q7UCQ2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase;
DE            Short=Gamma-Glu-GABA hydrolase;
DE            EC=3.5.1.94;
GN   Name=puuD; OrderedLocusNames=SF1303, S1385;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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=AAN42914.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP16796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN42914.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP16796.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_707207.2; NC_004337.2.
DR   RefSeq; WP_005049729.1; NZ_WPGW01000009.1.
DR   AlphaFoldDB; Q83LB6; -.
DR   SMR; Q83LB6; -.
DR   STRING; 198214.SF1303; -.
DR   MEROPS; C26.961; -.
DR   EnsemblBacteria; AAN42914; AAN42914; SF1303.
DR   EnsemblBacteria; AAP16796; AAP16796; S1385.
DR   GeneID; 1027800; -.
DR   GeneID; 58388621; -.
DR   KEGG; sfl:SF1303; -.
DR   KEGG; sfx:S1385; -.
DR   PATRIC; fig|198214.7.peg.1529; -.
DR   HOGENOM; CLU_030756_0_0_6; -.
DR   OrthoDB; 1628378at2; -.
DR   UniPathway; UPA00188; UER00883.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000272688"
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;  28126 MW;  F0D1F71DEDC51F42 CRC64;
     MENIMNNPVI GVVMCRNRLK GHATQTLQEK YLNAIIHAGG LPIALPHALA EPSLLEQLLP
     KLDGIYLPSS PSNVQPHLYG ENGDEPDADP GRDLLSMAII NAALERRIPI FAICRGLQEL
     VVATGGSLHR KLCEQPELLE HREDPELPVE QQYAPSHEVQ VEEGGLLSAL LPECSNFWVN
     SLHGQGAKVV SPRLRVEARS PDGLVEAVSV INHPFALGVQ WHPEWNSSEY ALSRILFEGF
     ITAWQHHIAE KQRL