ID   NITR2_UNKP              Reviewed;         314 AA.
AC   Q6RWK4;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Nitrilase 2;
DE            EC=3.5.5.1;
DE   AltName: Full=Nitrilase II;
GN   ORFNames=BD5070;
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15066841; DOI=10.1128/aem.70.4.2429-2436.2004;
RA   Robertson D.E., Chaplin J.A., DeSantis G., Podar M., Madden M., Chi E.,
RA   Richardson T., Milan A., Miller M., Weiner D.P., Wong K., McQuaid J.,
RA   Farwell B., Preston L.A., Tan X., Snead M.A., Keller M., Mathur E.,
RA   Kretz P.L., Burk M.J., Short J.M.;
RT   "Exploring nitrilase sequence space for enantioselective catalysis.";
RL   Appl. Environ. Microbiol. 70:2429-2436(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=12148986; DOI=10.1021/ja0259842;
RA   DeSantis G., Zhu Z., Greenberg W.A., Wong K., Chaplin J., Hanson S.R.,
RA   Farwell B., Nicholson L.W., Rand C.L., Weiner D.P., Robertson D.E.,
RA   Burk M.J.;
RT   "An enzyme library approach to biocatalysis: development of nitrilases for
RT   enantioselective production of carboxylic acid derivatives.";
RL   J. Am. Chem. Soc. 124:9024-9025(2002).
CC   -!- FUNCTION: Nitrilases catalyze the mild hydrolytic conversion of
CC       organonitriles directly to the corresponding carboxylic acids.
CC       Catalyzes the production of aryllactic acid derivatives. Mediates the
CC       hydrolysis of cyanohydrin to (S)-phenyllactic acid.
CC       {ECO:0000269|PubMed:12148986}.
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; AY487498; AAR97445.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6RWK4; -.
DR   SMR; Q6RWK4; -.
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   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..314
FT                   /note="Nitrilase 2"
FT                   /id="PRO_0000422218"
FT   DOMAIN          7..269
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        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   314 AA;  34283 MW;  6F19DDDADF8AC2D3 CRC64;
     MGEFGEVTLG VAQAAPVYFD REASTEKARG LIREAGEKGV DLLAFGETWL TGYPYWKDAP
     WSREYNDLRA RYVANGVMIP GPETDALCQA AAEAGVDVAI GVVELEPGSL SSVYCTLLFI
     SREGEILGRH RKLKPTDSER RYWSEGDATG LRVYERPYGR LSGLNCWEHL MMLPGYALAA
     QGTQFHVAAW PNMASSASEL LSRAYAYQAG CYVLCAGGLG PAPGELPDGI AAESLDHLTG
     ESCIIDPWGK VIAGPVSCEE TLITARVSTA SIYRRKSLTD VGGHYSRPDV FRFEVDRSER
     PRVVFRDGDV DDRG