AMIE_MARN8
ID AMIE_MARN8 Reviewed; 348 AA.
AC A1U7G1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Maqu_3862;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(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; CP000514; ABM20930.1; -; Genomic_DNA.
DR RefSeq; WP_011787263.1; NC_008740.1.
DR AlphaFoldDB; A1U7G1; -.
DR SMR; A1U7G1; -.
DR STRING; 351348.Maqu_3862; -.
DR EnsemblBacteria; ABM20930; ABM20930; Maqu_3862.
DR KEGG; maq:Maqu_3862; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_071797_0_0_6; -.
DR OMA; PWVPIEG; -.
DR OrthoDB; 1650683at2; -.
DR Proteomes; UP000000998; 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;
KW Hydrolase.
FT CHAIN 1..348
FT /note="Aliphatic amidase"
FT /id="PRO_1000067049"
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 348 AA; 38461 MW; 99B9AB1262504DAE CRC64;
MRHGDISSSN DTVGVAVVNY KMPRLHTKAE VLDNARKIAD IIKGMKVGLP GMDLVVFPEY
STMGIMYDND EMMETAATIP GDETAIFSAA CREANTWGVF SLTGERHEDH PNKAPYNTLV
LINNEGEIVQ KYRKCIPWCP IEGWYPGDTT YVTEGPKGMK ISLIICDDGN YPEIWRDCAM
KGAELIVRCQ GYMYPAKEQQ IMMAKSMAWA NNCYVAVANA SGFDGVYSYF GHSAIIGFDG
RTLGECGEED MGVQYAQLSV SQIRDARAND QSQNHLFKLL HRGYTGVHNS GDGDKGVADC
PFEFYRTWVM DAQKAQENVE AMTRKTVGTA ECPVGELPFD GKEKTAGA
