ID   AMIE_PSEA7              Reviewed;         346 AA.
AC   A6V262;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=PSPA7_1764;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR82057.1; -; Genomic_DNA.
DR   RefSeq; WP_012074883.1; NC_009656.1.
DR   AlphaFoldDB; A6V262; -.
DR   SMR; A6V262; -.
DR   EnsemblBacteria; ABR82057; ABR82057; PSPA7_1764.
DR   KEGG; pap:PSPA7_1764; -.
DR   HOGENOM; CLU_071797_0_0_6; -.
DR   OMA; PWVPIEG; -.
DR   OrthoDB; 1650683at2; -.
DR   Proteomes; UP000001582; 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..346
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_1000067051"
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:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01242"
SQ   SEQUENCE   346 AA;  38495 MW;  125DE8446E1AD063 CRC64;
     MRHGDISSSN DTVGVAVVNY KMPRLHTAAE VLDNARRIAD MIVGMKQGLP GMDLVVFPEY
     SLQGIMYDPA EMMETAVAIP GEETEIFSRA CRKANVWGVF SLTGERHEEH PRKAPYNTLV
     LIDNNGEIVQ KYRKIIPWCP IEGWYPGGQT YVSDGPKGMK ISLIICDDGN YPEIWRDCAM
     KGAELIVRCQ GYMYPAKDQQ VMMAKAMAWA NNCYVAVANA AGFDGVYSYF GHSAIIGFDG
     RTLGECGEEE MGIQYAQLSL SQIRDARAND QSQNHLFKIL HRGYSGLQAS GDGDRGLAEC
     PFEFYRTWVT DAEKARENVE RLTRSTTGVA QCPVGRLPYE GLEKEA