AMIE_BURCH
ID AMIE_BURCH Reviewed; 341 AA.
AC A0B137;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=Bcen2424_4629;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000459; ABK11363.1; -; Genomic_DNA.
DR RefSeq; WP_011547493.1; NC_008543.1.
DR AlphaFoldDB; A0B137; -.
DR SMR; A0B137; -.
DR KEGG; bch:Bcen2424_4629; -.
DR HOGENOM; CLU_071797_0_0_4; -.
DR OMA; PWVPIEG; -.
DR OrthoDB; 1650683at2; -.
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.
FT CHAIN 1..341
FT /note="Aliphatic amidase"
FT /id="PRO_1000067046"
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 341 AA; 38161 MW; C4FE4BC71A260074 CRC64;
MRHGDISSSR DCVGVAVVNY KMPRLHTKAE VLDNARRIAD MVVGMKQGLP GMDLVVFPEY
STHGIMYDRQ EMFDTASTIP GEETDIFAAA CRKANVWGVF SITGERHEAH PHKVPYNTLV
LIDNRGEIVQ KYRKIMPWTP IEGWYPGDRT YVTDGPKGLK ISLIICDDGN YPEIWRDCAM
NGAELIVRCQ GYMYPAKEQQ VMVAKAMAWM NNTYVAVANA TGWDGVYSYF GHSAIVGFDG
RTLGECGEEE MGVQYAELSL GMIRDARRNM QSQNHLYKLL HRGYTGTINS GDGVNGVAEC
PFGFYRDWIT DPDATRRRVE ALTRTTPGTP ECPIEGIPHE G
