ID   HIPO_CAMJE              Reviewed;         383 AA.
AC   P45493; Q0P9R7; Q9PNV4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Hippurate hydrolase {ECO:0000305};
DE            EC=3.5.1.32 {ECO:0000269|PubMed:7730270};
DE   AltName: Full=Benzoylglycine amidohydrolase {ECO:0000303|PubMed:7730270};
DE   AltName: Full=Hippuricase {ECO:0000303|PubMed:7730270};
GN   Name=hipO {ECO:0000303|PubMed:7730270}; OrderedLocusNames=Cj0985c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX   PubMed=7730270; DOI=10.1128/jb.177.9.2396-2402.1995;
RA   Hani E.K., Chan V.L.;
RT   "Expression and characterization of Campylobacter jejuni benzoylglycine
RT   amidohydrolase (Hippuricase) gene in Escherichia coli.";
RL   J. Bacteriol. 177:2396-2402(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Cleaves hippuric acid into benzoic acid and glycine.
CC       {ECO:0000269|PubMed:7730270}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-benzoylglycine = benzoate + glycine;
CC         Xref=Rhea:RHEA:10424, ChEBI:CHEBI:15377, ChEBI:CHEBI:16150,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:606565; EC=3.5.1.32;
CC         Evidence={ECO:0000269|PubMed:7730270};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; Z36940; CAA85396.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL35103.1; -; Genomic_DNA.
DR   PIR; F81373; F81373.
DR   PIR; I40762; I40762.
DR   RefSeq; WP_002853394.1; NC_002163.1.
DR   RefSeq; YP_002344380.1; NC_002163.1.
DR   AlphaFoldDB; P45493; -.
DR   SMR; P45493; -.
DR   IntAct; P45493; 5.
DR   STRING; 192222.Cj0985c; -.
DR   PaxDb; P45493; -.
DR   PRIDE; P45493; -.
DR   EnsemblBacteria; CAL35103; CAL35103; Cj0985c.
DR   GeneID; 905276; -.
DR   KEGG; cje:Cj0985c; -.
DR   PATRIC; fig|192222.6.peg.968; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_1_1_7; -.
DR   OMA; EWHHPAF; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0047980; F:hippurate hydrolase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR11014; PTHR11014; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..383
FT                   /note="Hippurate hydrolase"
FT                   /id="PRO_0000061954"
FT   CONFLICT        125
FT                   /note="A -> T (in Ref. 1; CAA85396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="I -> V (in Ref. 1; CAA85396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250
FT                   /note="A -> V (in Ref. 1; CAA85396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="I -> L (in Ref. 1; CAA85396)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  42547 MW;  01C94C1293F6B1C8 CRC64;
     MNLIPEILDL QGEFEKIRHQ IHENPELGFD ELCTAKLVAQ KLKEFGYEVY EEIGKTGVVG
     VLKKGNSDKK IGLRADMDAL PLQECTNLPY KSKKENVMHA CGHDGHTTSL LLAAKYLASQ
     NFNGALNLYF QPAEEGLGGA KAMIEDGLFE KFDSDYVFGW HNMPFGSDKK FYLKKGAMMA
     SSDSYSIEVI GRGGHGSAPE KAKDPIYAAS LLIVALQSIV SRNVDPQNSA VVSIGAFNAG
     HAFNIIPDIA TIKMSVRALD NETRKLTEEK IYKICKGIAQ ANDIEIKINK NVVAPVTMNN
     DEAVDFASEV AKELFGEKNC EFNHRPLMAS EDFGFFCEMK KCAYAFLENE NDIYLHNSSY
     VFNDKLLARA ASYYAKLALK YLK