ID   AMIE_HELPY              Reviewed;         339 AA.
AC   O25067; O32644;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Aliphatic amidase;
DE            EC=3.5.1.4;
DE   AltName: Full=Acylamide amidohydrolase;
GN   Name=amiE; OrderedLocusNames=HP_0294;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 96-106 AND 160-174,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=85P;
RX   PubMed=9364923; DOI=10.1111/j.1365-2958.1997.mmi536.x;
RA   Skouloubris S., Labigne A., De Reuse H.;
RT   "Identification and characterization of an aliphatic amidase in
RT   Helicobacter pylori.";
RL   Mol. Microbiol. 25:989-998(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND MUTAGENESIS OF CYS-165 AND ASP-167.
RX   PubMed=11359566; DOI=10.1046/j.1365-2958.2001.02400.x;
RA   Skouloubris S., Labigne A., De Reuse H.;
RT   "The AmiE aliphatic amidase and AmiF formamidase of Helicobacter pylori:
RT   natural evolution of two enzyme paralogues.";
RL   Mol. Microbiol. 40:596-609(2001).
RN   [4]
RP   TRANSCRIPTIONAL REGULATION.
RX   PubMed=12499381; DOI=10.1074/jbc.m207542200;
RA   van Vliet A.H.M., Stoof J., Poppelaars S.W., Bereswill S., Homuth G.,
RA   Kist M., Kuipers E.J., Kusters J.G.;
RT   "Differential regulation of amidase- and formamidase-mediated ammonia
RT   production by the Helicobacter pylori fur repressor.";
RL   J. Biol. Chem. 278:9052-9057(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC       their corresponding organic acids with release of ammonia. Hydrolyzes
CC       propionamide, acetamide and acrylamide, but has no activity with
CC       formamide or urea. The natural substrates of AmiE in its gastric
CC       environment are not known. Probably functions to ensure nitrogen supply
CC       to the bacteria.
CC   -!- FUNCTION: Also exhibits in vitro acyl transferase activity,
CC       transferring the acyl moiety of short-chain amides to hydroxylamine to
CC       form hydroxamates. The highest level of acyl transfer activity is
CC       observed with acetamide.
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:0000269|PubMed:11359566, ECO:0000269|PubMed:9364923};
CC   -!- ACTIVITY REGULATION: Inhibited by iodoacetate.
CC       {ECO:0000269|PubMed:11359566}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|PubMed:11359566};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:11359566};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11359566}.
CC   -!- INDUCTION: Repressed by iron via the binding of the Fur protein to the
CC       amiE promoter. {ECO:0000269|PubMed:12499381}.
CC   -!- MISCELLANEOUS: Asp-167 is probably not involved in the catalytic
CC       mechanism, but is probably involved instead in maintenance of the
CC       structural integrity of the amidase. {ECO:0000305|PubMed:11359566}.
CC   -!- MISCELLANEOUS: Expression of the amiE gene is stimulated in a mutant
CC       deficient in urease activity, suggesting that production of this enzyme
CC       is regulated to maintain intracellular nitrogen balance in H.pylori.
CC       {ECO:0000305|PubMed:9364923}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000305}.
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DR   EMBL; Y12252; CAA72932.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07363.1; -; Genomic_DNA.
DR   PIR; F64556; F64556.
DR   RefSeq; NP_207092.1; NC_000915.1.
DR   RefSeq; WP_001215729.1; NC_018939.1.
DR   AlphaFoldDB; O25067; -.
DR   SMR; O25067; -.
DR   IntAct; O25067; 7.
DR   MINT; O25067; -.
DR   STRING; 85962.C694_01485; -.
DR   PaxDb; O25067; -.
DR   EnsemblBacteria; AAD07363; AAD07363; HP_0294.
DR   KEGG; hpy:HP_0294; -.
DR   PATRIC; fig|85962.47.peg.314; -.
DR   eggNOG; COG0388; Bacteria.
DR   OMA; PWVPIEG; -.
DR   PhylomeDB; O25067; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IMP:CACAO.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Reference proteome.
FT   CHAIN           1..339
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_0000204058"
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:0000250"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         165
FT                   /note="C->S,A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11359566"
FT   MUTAGEN         167
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11359566"
FT   CONFLICT        29..30
FT                   /note="NE -> EQ (in Ref. 1; CAA72932)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="A -> D (in Ref. 1; CAA72932)"
FT                   /evidence="ECO:0000305"
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