ID   AMI3_MYCLE              Reviewed;         468 AA.
AC   O33040;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Putative amidase AmiC;
DE            EC=3.5.1.4;
GN   Name=amiC; OrderedLocusNames=ML1596; ORFNames=MLCB250.65;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; Z97369; CAB10659.1; -; Genomic_DNA.
DR   EMBL; AL583922; CAC30547.1; -; Genomic_DNA.
DR   PIR; F87108; F87108.
DR   RefSeq; NP_302099.1; NC_002677.1.
DR   RefSeq; WP_010908420.1; NC_002677.1.
DR   AlphaFoldDB; O33040; -.
DR   SMR; O33040; -.
DR   STRING; 272631.ML1596; -.
DR   EnsemblBacteria; CAC30547; CAC30547; CAC30547.
DR   KEGG; mle:ML1596; -.
DR   PATRIC; fig|272631.5.peg.3009; -.
DR   Leproma; ML1596; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_4_11; -.
DR   OMA; WNTDHTA; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..468
FT                   /note="Putative amidase AmiC"
FT                   /id="PRO_0000105257"
FT   ACT_SITE        80
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  51164 MW;  A8E048D702F6A234 CRC64;
     MQRVHAFGDD ALGDLDAVGL ADAIRAGWVS RADVIEAAIV RTEAVNPALG GLAYEAFQWA
     RQTASKAGSG FFSGVPTFIK DNIDVAGQPT MRGSDAWVPR NAFDDGEFTR LYLATGPVSL
     GKTQLSEFGF SASAEHMRLG PVRNPWDTDY TAGASSSGSG AFVAAGVVPM AHANDGGGSI
     RIPASCNGLV GLKPSRGRLP LDSELRRLPV GIVVNGVLTR SVRDTAAFYR EAERIWHNPK
     LPPVGDVTQP GRQRLRIAVV TRSVQRECSP ELRELTLKSA RLLEELGHRV ERVAEPPVPP
     NFPDDFLLYW GLLAAMQVRT GRLAFGNTFD RTKLDSLTLG LDRHASRNMH RLPKAIMRLR
     RLRRRTADFF ATYDVLLTPT VADETPRIGY LTPTDYQQVM DRLMGWVAFT PLQNVTGEPA
     ISLPLAQSAD GMPVGMMFTA DFGQEAQLLE LAFELEEARP WARIQIGD