(data stored in ACNUC1104 zone)

SWISSPROT: AMIE_RHOE4

ID   AMIE_RHOE4              Reviewed;         345 AA.
AC   C0ZNE8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 54.
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=RER_04920;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) 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}.
DR   EMBL; AP008957; BAH31200.1; -; Genomic_DNA.
DR   RefSeq; WP_019746630.1; NC_012490.1.
DR   SMR; C0ZNE8; -.
DR   STRING; 234621.RER_04920; -.
DR   EnsemblBacteria; BAH31200; BAH31200; RER_04920.
DR   GeneID; 31540339; -.
DR   KEGG; rer:RER_04920; -.
DR   eggNOG; ENOG4105DCY; Bacteria.
DR   eggNOG; COG0388; LUCA.
DR   HOGENOM; HOG000077502; -.
DR   KO; K01426; -.
DR   OMA; RIWGCFS; -.
DR   Proteomes; UP000002204; 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;
DR   PRODOM; C0ZNE8.
DR   SWISS-2DPAGE; C0ZNE8.
KW   Hydrolase.
FT   CHAIN           1..345
FT                   /note="Aliphatic amidase"
FT                   /id="PRO_1000214091"
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;  38200 MW;  A3C87F4073F689FE CRC64;
     MRHGDISSSN DTVGVAVVNY KMPRLHDRAG VLENARKIAD MMIGMKTGLP GMDLVVFPEY
     STQGIMYNEE EMYATAATIP GDETAIFSAA CREADTWGIF SITGEQHEDH PNKPPYNTLI
     LIDNKGEIVQ KYRKILPWCP IEGWYPGDTT YVSEGPKGLK ISLIICDDGN YPEIWRDCAM
     KGAELIVRCQ GYMYPAKDQQ VMMSKAMAWA NNCYVAVANA AGFDGVYSYF GHSAIIGFDG
     RTLGETGEEE YGIQYAQLSV SAIRDAREND QSQNHIFKLL HRGYSGVHAA GDGDKGVADC
     PFEFYKLWVT DAQKAQERVE AITRDTVGVA DCRVGNLPVE KTIEV
//

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