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Aliphatic amidase (EC 3.5.1.4) (Acylamide amidohydrolase) (Wide spectrum amidase)

 AMIE_RHOER              Reviewed;         345 AA.
Q01360;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 66.
RecName: Full=Aliphatic amidase;
EC=3.5.1.4;
AltName: Full=Acylamide amidohydrolase;
AltName: Full=Wide spectrum amidase;
Name=amiE; Synonyms=amiP;
Rhodococcus erythropolis (Arthrobacter picolinophilus).
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
Rhodococcus.
NCBI_TaxID=1833;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
STRAIN=Brevibacterium sp. R312;
PubMed=1628849; DOI=10.1016/0378-1119(92)90635-3;
Soubrier F., Levy-Schil S., Mayaux J.F., Petre D., Arnaud A.,
Crouzet J.;
"Cloning and primary structure of the wide-spectrum amidase from
Brevibacterium sp. R312: high homology to the amiE product from
Pseudomonas aeruginosa.";
Gene 116:99-104(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hjort C.M., Woeldike H.F., Emborg C.;
"Cloning and expression of an aliphatic amidase from Rhodococcus
erythropolis in E. coli and R. erythropolis using a new R.
erythropolis transformation system.";
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
STRAIN=Brevibacterium sp. R312;
Fournand D., Arnaud A., Galzy P.;
"Study of the acyl transfer activity of a recombinant amidase
overproduced in an Escherichia coli strain. Application for short-
chain hydroxamic acid and acid hydrazide synthesis.";
J. Mol. Catal., B Enzym. 4:77-90(1998).
-!- FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides
to their corresponding organic acids with release of ammonia.
Hydrolyzes propionamide, acetamide and acrylamide. Enables the
organism to use such amides as both carbon and nitrogen source.
{ECO:0000269|Ref.3}.
-!- FUNCTION: Also exhibits in vitro acyl transferase activity,
transferring the acyl moiety of short-chain amides to
hydroxylamine or hydrazine to form hydroxamates and acid
hydrazides respectively. The highest level of acyl transfer
activity is observed with acetamide. {ECO:0000269|Ref.3}.
-!- CATALYTIC ACTIVITY: A monocarboxylic acid amide + H(2)O = a
monocarboxylate + NH(3).
-!- SUBUNIT: Homotetramer.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
Aliphatic amidase family. {ECO:0000305}.
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EMBL; M76451; AAA22990.1; -; Genomic_DNA.
EMBL; M88614; AAA26186.1; -; Genomic_DNA.
ProteinModelPortal; Q01360; -.
SMR; Q01360; -.
eggNOG; ENOG4105DCY; Bacteria.
eggNOG; COG0388; LUCA.
GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
Gene3D; 3.60.110.10; -; 1.
HAMAP; MF_01242; Aliphatic_amidase; 1.
InterPro; IPR023719; Aliphatic_amidase.
InterPro; IPR003010; C-N_Hydrolase.
InterPro; IPR036526; C-N_Hydrolase_sf.
Pfam; PF00795; CN_hydrolase; 1.
SUPFAM; SSF56317; SSF56317; 1.
PROSITE; PS50263; CN_HYDROLASE; 1.
1: Evidence at protein level;
Direct protein sequencing; Hydrolase.
CHAIN 1 345 Aliphatic amidase.
/FTId=PRO_0000204061.
DOMAIN 13 260 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 59 59 Proton acceptor. {ECO:0000250}.
ACT_SITE 134 134 Proton donor. {ECO:0000250}.
ACT_SITE 166 166 Nucleophile. {ECO:0000250}.
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


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