ID   AMIE_DELAS              Reviewed;         345 AA.
AC   A9C011;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-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=Daci_3641;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-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; CP000884; ABX36273.1; -; Genomic_DNA.
DR   RefSeq; WP_012205469.1; NC_010002.1.
DR   AlphaFoldDB; A9C011; -.
DR   SMR; A9C011; -.
DR   STRING; 398578.Daci_3641; -.
DR   PRIDE; A9C011; -.
DR   EnsemblBacteria; ABX36273; ABX36273; Daci_3641.
DR   GeneID; 60687881; -.
DR   KEGG; dac:Daci_3641; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_071797_0_0_4; -.
DR   OMA; PWVPIEG; -.
DR   Proteomes; UP000000784; 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; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_1000139805"
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   345 AA;  38565 MW;  CC363F466F5921EC CRC64;
     MRHGDISSSN DCVGVAVVNY KMPRLHTKAE VLDNCRKIAD MLVGMKRGLP GMDLVIFPEY
     STHGIMYDAK EMYDTASAIP GEETEIFADA CRRANVWGVF SLTGERHEEH PNKAPYNTLI
     LMNNQGEIVQ KYRKIMPWVP IEGWYPGDCT YVSEGPKGLK ISLIICDDGN YPEIWRDCAM
     RGAELVVRCQ GYMYPAKEQQ IMVSKAMAFM NNCYVAVANA AGFDGVYSYF GHSAIIGFDG
     RTLGETGEEE MGIQYAELSK HLIRDARKNG QSQNHLFKLV HRGYTGTINS GDGDKGVAAC
     PYNFYSQWVN DPEGTREMVE SFTRTTVGTP ECPIEGIPHE APKHR