ID   NITR3_UNKP              Reviewed;         330 AA.
AC   Q6RWG0;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Nitrilase 3;
DE            EC=3.5.5.1;
DE   AltName: Full=Nitrilase III;
GN   ORFNames=BD5308;
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       {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; AY487542; AAR97489.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6RWG0; -.
DR   SMR; Q6RWG0; -.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..330
FT                   /note="Nitrilase 3"
FT                   /id="PRO_0000422219"
FT   DOMAIN          4..273
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          310..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        44
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   330 AA;  35680 MW;  F416637668CC0ABC CRC64;
     MKVVKAAAVQ ISPVLYSREA TVEKVVKKIH ELGQLGVQFA TFPETVVPYY PYFSAVQTGI
     ELLSGTEHLR LLDQAVTVPS PATDAIGEAA RKAGMVVSIG VNERDGGTLY NTQLLFDADG
     TLIQRRRKIT PTHFERMIWG QGDGSGLRAV DSKVGRIGQL ACFEHNNPLA RYALIADGEQ
     IHSAMYPGSA FGEGFAQRME INIRQHALES GAFVVNATAW LDADQQAQII KDTGCGIGPI
     SGGCFTTIVA PDGMLMAEPL RSGEGEVIVD LDFTLIDRRK MLMDSAGHYN RPELLSLMID
     RTATAHVHER AAHPVSGAEQ GPEDLRTPAA