ID   NITR2_BRADU             Reviewed;         321 AA.
AC   Q89PT3;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Nitrilase blr3397;
DE            EC=3.5.5.7;
GN   OrderedLocusNames=blr3397;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=18061298; DOI=10.1016/j.jbiotec.2007.10.001;
RA   Zhu D., Mukherjee C., Yang Y., Rios B.E., Gallagher D.T., Smith N.N.,
RA   Biehl E.R., Hua L.;
RT   "A new nitrilase from Bradyrhizobium japonicum USDA 110. Gene cloning,
RT   biochemical characterization and substrate specificity.";
RL   J. Biotechnol. 133:327-333(2008).
CC   -!- FUNCTION: Nitrilase that acts on various kinds of nitrile compounds
CC       such as aliphatic and aromatic nitriles. Has higher activity toward
CC       aliphatic nitriles compared to aromatic nitriles. Among the different
CC       substrates tested, has the highest activity toward hydrocinnamonitrile.
CC       {ECO:0000269|PubMed:18061298}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic nitrile + 2 H2O = a carboxylate + NH4(+);
CC         Xref=Rhea:RHEA:46188, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:80291; EC=3.5.5.7;
CC         Evidence={ECO:0000269|PubMed:18061298};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.36 mM for phenylacetonitrile {ECO:0000269|PubMed:18061298};
CC         Note=kcat is 111 min(-1) with phenylacetonitrile.;
CC       pH dependence:
CC         Optimum pH is 7.0-8-0. {ECO:0000269|PubMed:18061298};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:18061298};
CC   -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:18061298}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; BA000040; BAC48662.1; -; Genomic_DNA.
DR   RefSeq; NP_770037.1; NC_004463.1.
DR   RefSeq; WP_011086181.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89PT3; -.
DR   SMR; Q89PT3; -.
DR   STRING; 224911.27351656; -.
DR   EnsemblBacteria; BAC48662; BAC48662; BAC48662.
DR   GeneID; 64023145; -.
DR   KEGG; bja:blr3397; -.
DR   PATRIC; fig|224911.44.peg.3047; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_030130_6_1_5; -.
DR   InParanoid; Q89PT3; -.
DR   OMA; PKGLDFG; -.
DR   PhylomeDB; Q89PT3; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0018762; F:aliphatic nitrilase activity; IDA:UniProtKB.
DR   GO; GO:0000257; F:nitrilase activity; IBA:GO_Central.
DR   GO; GO:0018822; F:nitrile hydratase activity; IBA:GO_Central.
DR   GO; GO:0051410; P:detoxification of nitrogen compound; IBA:GO_Central.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
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.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..321
FT                   /note="Nitrilase blr3397"
FT                   /id="PRO_0000422217"
FT   DOMAIN          10..277
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT                   ECO:0000255|PROSITE-ProRule:PRU10105"
SQ   SEQUENCE   321 AA;  34475 MW;  561F3156D4BF8B86 CRC64;
     MMDSNRPNTY KAAVVQAASD PTSSLVSAQK AAALIEKAAG AGARLVVFPE AFIGGYPKGN
     SFGAPVGMRK PEGREAFRLY WEAAIDLDGV EVETIAAAAA ATGAFTVIGC IEREQGTLYC
     TALFFDGARG LVGKHRKLMP TAGERLIWGF GDGSTMPVFE TSLGNIGAVI CWENYMPMLR
     MHMYSQGISI YCAPTADDRD TWLPTMQHIA LEGRCFVLTA CQHLKRGAFP ADYECALGAD
     PETVLMRGGS AIVNPLGKVL AGPCFEGETI LYADIALDEV TRGKFDFDAA GHYSRPDVFQ
     LVVDDRPKRA VSTVSAVRAR N