ID AMIE_VARPS Reviewed; 344 AA.
AC C5CWZ4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Vapar_0135;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS16798.1; -; Genomic_DNA.
DR AlphaFoldDB; C5CWZ4; -.
DR SMR; C5CWZ4; -.
DR STRING; 543728.Vapar_0135; -.
DR KEGG; vap:Vapar_0135; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_4; -.
DR OrthoDB; 9803803at2; -.
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 CDD; cd07565; aliphatic_amidase; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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 PANTHER; PTHR43674:SF14; ALIPHATIC AMIDASE; 1.
DR PANTHER; PTHR43674; NITRILASE C965.09-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..344
FT /note="Aliphatic amidase"
FT /id="PRO_1000214092"
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 344 AA; 38195 MW; D4BCBBA653E80A56 CRC64;
MRHGDISSSN DCVGVAVVNY KMPRLHTKAE VLDNARKIGE MLVGMKKGLP GMDLVIFPEY
STHGIMYDTK EMYDTASAIP GEETAIFADA CRRANVWGVF SLTGERHEAH PDKAPYNTLI
LMNNQGEIVQ KYRKIMPWVP IEGWYPGDCT YVSDGPKGMK MSLIICDDGN YPEIWRDCAM
RGAELIIRCQ GYMYPAKEQQ ILVSKAMAFM NNTYVAVANA AGFDGVYSYF GHSAIIGFDG
RTLGECGEEE MGINYAELSM GLIRDARRNG QSQNHLFKLM HRGYTGVIHS GDGDKGVAAC
PFDFYKQWIN DPEGAREQVE SFTRSTIGTA ECPIEGLPNE AARS
//
