ID   NRL_BACSX               Reviewed;         339 AA.
AC   P82605;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Nitrilase;
DE            EC=3.5.5.1;
GN   Name=nit;
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14.
RX   PubMed=10651646; DOI=10.1021/bi991598u;
RA   Kato Y., Nakamura K., Sakiyama H., Mayhew S.G., Asano Y.;
RT   "Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus
RT   sp. strain OxB-1: purification, characterization, and molecular cloning of
RT   the gene.";
RL   Biochemistry 39:800-809(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nitrile + 2 H2O = a carboxylate + NH4(+);
CC         Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1;
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; AB028892; BAA90460.1; -; Genomic_DNA.
DR   AlphaFoldDB; P82605; -.
DR   SMR; P82605; -.
DR   STRING; 98228.OXB_1096; -.
DR   BRENDA; 3.5.5.1; 16272.
DR   GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07564; nitrilases_CHs; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
DR   InterPro; IPR044149; Nitrilases_CHs.
DR   PANTHER; PTHR46044; PTHR46044; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00920; NITRIL_CHT_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10651646"
FT   CHAIN           2..339
FT                   /note="Nitrilase"
FT                   /id="PRO_0000204043"
FT   DOMAIN          7..277
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        162
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   339 AA;  37784 MW;  C47A9601BBCE7275 CRC64;
     MSNYPKYRVA AVQASPVLLD LDATIDKTCR LVDEAAANGA KVIAFPEAFI PGYPWWIWLG
     NADYGMKYYI QLYKNSVEIP SLAVQKLSSA GTNKVYFCVS VTEKDGGSLY LTQLWFDPNG
     DLIGKHRKLK ATNAEKTIWG DGDGSMMPVF ETEFGNLGGL QCWEHFLPLN VAAMASMNEQ
     VHVASWPIGM PQEGHLFGPE QCVTATKYYA ISNQVFCLLS SQIWTEEQRD KICETEEQRN
     FMKVGHGFSK IIAPNGMEIG NKLAHDEEGI TYADIDLEQI IPGKFLIDSA GHYSTPGFLS
     LSFDRTEKKP IKHIGESAQE TVTYEEIQYG NKANVKVHS