ID   AMIE_HELPG              Reviewed;         339 AA.
AC   B5ZA60;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Aliphatic amidase {ECO:0000255|HAMAP-Rule:MF_01242};
DE            EC=3.5.1.4 {ECO:0000255|HAMAP-Rule:MF_01242};
DE   AltName: Full=Acylamide amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01242};
GN   Name=amiE {ECO:0000255|HAMAP-Rule:MF_01242}; OrderedLocusNames=HPG27_273;
OS   Helicobacter pylori (strain G27).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=563041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G27;
RX   PubMed=18952803; DOI=10.1128/jb.01416-08;
RA   Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA   Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT   "The complete genome sequence of Helicobacter pylori strain G27.";
RL   J. Bacteriol. 191:447-448(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC       their corresponding organic acids with release of ammonia.
CC       {ECO:0000255|HAMAP-Rule:MF_01242}.
CC   -!- FUNCTION: Also exhibits in vitro acyl transferase activity,
CC       transferring the acyl moiety of short-chain amides to hydroxylamine to
CC       form hydroxamates. {ECO:0000255|HAMAP-Rule:MF_01242}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC         NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01242};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000255|HAMAP-Rule:MF_01242}.
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DR   EMBL; CP001173; ACI27040.1; -; Genomic_DNA.
DR   RefSeq; WP_001215729.1; NC_011333.1.
DR   AlphaFoldDB; B5ZA60; -.
DR   SMR; B5ZA60; -.
DR   EnsemblBacteria; ACI27040; ACI27040; HPG27_273.
DR   KEGG; hpg:HPG27_273; -.
DR   HOGENOM; CLU_071797_0_0_7; -.
DR   OMA; PWVPIEG; -.
DR   OrthoDB; 1650683at2; -.
DR   Proteomes; UP000001735; Chromosome.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   HAMAP; MF_01242; Aliphatic_amidase; 1.
DR   InterPro; IPR023719; Aliphatic_amidase.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..339
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_1000139807"
FT   DOMAIN          13..259
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        59
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
SQ   SEQUENCE   339 AA;  37713 MW;  7F70580FC7B50A92 CRC64;
     MRHGDISSSP DTVGVAVVNY KMPRLHTKNE VLENCRNIAK VIGGVKQGLP GLDLIIFPEY
     STHGIMYDRQ EMFDTAASVP GEETAIFAEA CKKNKVWGVF SLTGEKHEQA KKNPYNTLIL
     VNDKGEIVQK YRKILPWCPI ECWYPGDKTY VVDGPKGLKV SLIICDDGNY PEIWRDCAMR
     GAELIVRCQG YMYPAKEQQI AIVKAMAWAN QCYVAVANAT GFDGVYSYFG HSSIIGFDGH
     TLGECGEEEN GLQYAQLSVQ QIRDARKYDQ SQNQLFKLLH RGYSGVFASG DGDKGVAECP
     FEFYKTWVND PKKAQENVEK ITRPSVGVAA CPVGDLPTK