ID   AMIE_NOCFA              Reviewed;         345 AA.
AC   Q5Z1U0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=NFA_7560;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD55601.1; -; Genomic_DNA.
DR   RefSeq; WP_011207287.1; NC_006361.1.
DR   AlphaFoldDB; Q5Z1U0; -.
DR   SMR; Q5Z1U0; -.
DR   STRING; 247156.NFA_7560; -.
DR   EnsemblBacteria; BAD55601; BAD55601; NFA_7560.
DR   GeneID; 61131588; -.
DR   KEGG; nfa:NFA_7560; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_071797_0_0_11; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000006820; 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_1000067050"
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;  38183 MW;  FB8F7CCA6B0FAC97 CRC64;
     MRHGDISSSP DTVGVAVVNY KMPRLHTKAE VLDNCRRIAD MLVGMKSGLP GMDLVVFPEY
     STQGIMYDEQ EMYDTAATVP GEETAIFSAA CREAGVWGVF SITGEQHEDH PRKPPYNTLV
     LIDDHGEIVQ KYRKILPWCP IEGWYPGDTT YVTEGPKGLK ISLIVCDDGN YPEIWRDCAM
     KGAELIVRCQ GYMYPSKDQQ VLMAKAMAWA NNCYVAVANA AGFDGVYSYF GHSALIGFDG
     RTLGETGEEE YGIQYAQLSI SAIRDARAHD QSQNHLFKLL HRGYSGVHAA GDGDRGVADC
     PFEFYKLWVT DAQQARERVE AITRDTVGVA DCRVGSLPVE QTLEA