ID   AMID_RHOER              Reviewed;         521 AA.
AC   P22984;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Amidase;
DE            EC=3.5.1.4;
GN   Name=amdA;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N-774;
RX   PubMed=2001397; DOI=10.1016/0167-4781(91)90058-t;
RA   Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.;
RT   "Cloning and characterization of an amidase gene from Rhodococcus species
RT   N-774 and its expression in Escherichia coli.";
RL   Biochim. Biophys. Acta 1088:225-233(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Brevibacterium sp. R312;
RX   PubMed=2254253; DOI=10.1128/jb.172.12.6764-6773.1990;
RA   Mayaux J.-F., Cerbelaud E., Soubrier F., Faucher D., Petre D.;
RT   "Purification, cloning, and primary structure of an enantiomer-selective
RT   amidase from Brevibacterium sp. strain R312: structural evidence for
RT   genetic coupling with nitrile hydratase.";
RL   J. Bacteriol. 172:6764-6773(1990).
CC   -!- FUNCTION: Hydrolyzes propionamides efficiently, and also at a lower
CC       efficiency, acetamide, acrylamide and indoleacetamide. This enzyme
CC       seems to be stereospecific and can lead to the production of a single
CC       enantiomer.
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; X54074; CAA38009.1; -; Genomic_DNA.
DR   EMBL; M60264; AAA62721.1; -; Genomic_DNA.
DR   AlphaFoldDB; P22984; -.
DR   SMR; P22984; -.
DR   STRING; 1833.XU06_28840; -.
DR   BRENDA; 3.5.1.4; 5389.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..521
FT                   /note="Amidase"
FT                   /id="PRO_0000105126"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        96
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   521 AA;  54706 MW;  9DF221A5D8D6B7EF CRC64;
     MATIRPDDKA IDAAARHYGI TLDKTARLEW PALIDGALGS YDVVDQLYAD EATPPTTSRE
     HAVPSASENP LSAWYVTTSI PPTSDGVLTG RRVAIKDNVT VAGVPMMNGS RTVEGFTPSR
     DATVVTRLLA AGATVAGKAV CEDLCFSGSS FTPASGPVRN PWDRQREAGG SSGGSAALVA
     NGDVDFAIGG DQGGSIRIPA AFCGVVGHKP TFGLVPYTGA FPIERTIDHL GPITRTVHDA
     ALMLSVIAGR DGNDPRQADS VEAGDYLSTL DSDVDGLRIG IVREGFGHAV SQPEVDDAVR
     AAAHSLTEIG CTVEEVNIPW HLHAFHIWNV IATDGGAYQM LDGNGYGMNA EGLYDPELMA
     HFASRRIQHA DALSETVKLV ALTGHHGITT LGGASYGKAR NLVPLARAAY DTALRQFDVL
     VMPTLPYVAS ELPAKDVDRA TFITKALGMI ANTAPFDVTG HPSLSVPAGL VNGLPVGMMI
     TGRHFDDATV LRVGRAFEKL RGAFPTPAER ASNSAPQLSP A