ID   AMIE_GEOSE              Reviewed;         348 AA.
AC   Q9RQ17;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Aliphatic amidase;
DE            EC=3.5.1.4;
DE   AltName: Full=Acylamide amidohydrolase;
DE   AltName: Full=Wide spectrum amidase;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-26.
RC   STRAIN=BR388;
RX   PubMed=10689071; DOI=10.1016/s0141-0229(99)00150-7;
RA   Cheong T.K., Oriel P.J.;
RT   "Cloning of a wide-spectrum amidase from Bacillus stearothermophilus BR388
RT   in Escherichia coli and marked enhancement of amidase expression using
RT   directed evolution.";
RL   Enzyme Microb. Technol. 26:152-158(2000).
CC   -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC       their corresponding organic acids with release of ammonia. Efficiently
CC       hydrolyzes propionamide, acetamide and acrylamide, but shows a very
CC       weak activity with aromatic and longer chain aliphatic amides.
CC       {ECO:0000269|PubMed:10689071}.
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:0000250}.
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:10689071};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|PubMed:10689071};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:10689071};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000305}.
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DR   EMBL; AF136599; AAF14257.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RQ17; -.
DR   SMR; Q9RQ17; -.
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   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..348
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_0000204056"
FT   DOMAIN          13..260
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        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         26
FT                   /note="H->R: 23-fold increase in activity due to increase
FT                   in amidase gene transcription."
FT                   /evidence="ECO:0000269|PubMed:10689071"
SQ   SEQUENCE   348 AA;  39085 MW;  2B421275E6DD8976 CRC64;
     MRHGDISSSH DTVGVAVVNY KMPRLHTKKE VIENAKNIAN MIVGMKQGLP GMDLVIFPEY
     STMGIMYDRK EMFETATTIP GPETEIFAEA CRKANTWGVF SLTGEQHEEH PHKNPYNTLV
     LINNKGEIVQ KYRKIIPWCP IEGWYPGDTT YVTEGPKGIK ISLIICDDGN YPEIWRDCAM
     KGAELIVRCQ GYMYPAKEQQ IMMAKTMAWA NNVYVAVANA TGFDGVYSYF GHSAIIGFDG
     RTLGECGEEE NGIQYAEISL SQIRDFRQNA QSQNHLFKLL HRGYTGIIQS GEGDKGVAEC
     PFDFYRTWVM DAEKARENVE KITRTTIGTA ECPIEGIPHE GKEKEASV