ID   AMIE_RHOER              Reviewed;         345 AA.
AC   Q01360;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Aliphatic amidase;
DE            EC=3.5.1.4;
DE   AltName: Full=Acylamide amidohydrolase;
DE   AltName: Full=Wide spectrum amidase;
GN   Name=amiE; Synonyms=amiP;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC   STRAIN=Brevibacterium sp. R312;
RX   PubMed=1628849; DOI=10.1016/0378-1119(92)90635-3;
RA   Soubrier F., Levy-Schil S., Mayaux J.F., Petre D., Arnaud A., Crouzet J.;
RT   "Cloning and primary structure of the wide-spectrum amidase from
RT   Brevibacterium sp. R312: high homology to the amiE product from Pseudomonas
RT   aeruginosa.";
RL   Gene 116:99-104(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hjort C.M., Woeldike H.F., Emborg C.;
RT   "Cloning and expression of an aliphatic amidase from Rhodococcus
RT   erythropolis in E. coli and R. erythropolis using a new R. erythropolis
RT   transformation system.";
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RC   STRAIN=Brevibacterium sp. R312;
RA   Fournand D., Arnaud A., Galzy P.;
RT   "Study of the acyl transfer activity of a recombinant amidase overproduced
RT   in an Escherichia coli strain. Application for short-chain hydroxamic acid
RT   and acid hydrazide synthesis.";
RL   J. Mol. Catal., B Enzym. 4:77-90(1998).
CC   -!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to
CC       their corresponding organic acids with release of ammonia. Hydrolyzes
CC       propionamide, acetamide and acrylamide. Enables the organism to use
CC       such amides as both carbon and nitrogen source. {ECO:0000269|Ref.3}.
CC   -!- FUNCTION: Also exhibits in vitro acyl transferase activity,
CC       transferring the acyl moiety of short-chain amides to hydroxylamine or
CC       hydrazine to form hydroxamates and acid hydrazides respectively. The
CC       highest level of acyl transfer activity is observed with acetamide.
CC       {ECO:0000269|Ref.3}.
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   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000305}.
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DR   EMBL; M76451; AAA22990.1; -; Genomic_DNA.
DR   EMBL; M88614; AAA26186.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01360; -.
DR   SMR; Q01360; -.
DR   STRING; 1833.XU06_02570; -.
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   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..345
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_0000204061"
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"
SQ   SEQUENCE   345 AA;  38200 MW;  176BDE82E6980247 CRC64;
     MRHGDISSSN DTVGVAVVNY KMPRLHDRAG VLENARKIAD MMIGMKTGLP GMDLVVFPEY
     STQGIMYNEE EMYATAATIP GDETAIFSAA CREADTWGIF SITGEQHEDH PNKPPYNTLI
     LIDNKGEIVQ RYRKILPWCP IEGWYPGDTT YVTEGPKGLK ISLIICDDGN YPEIWRDCAM
     KGAELIVRCQ GYMYPAKDQQ VMMSKAMAWA NNCYVAVANA AGFDGVYSYF GHSAIIGFDG
     RTLGETGEEE YGIQYAQLSV SAIRDAREND QSQNHIFKLL HRGYSGVHAA GDGDKGVADC
     PFEFYKLWVT DAQKAQERVE AITRDTVGVA DCRVGNLPVE KTVEA