ID   NRLB_KLEPO              Reviewed;         349 AA.
AC   P10045;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Nitrilase, bromoxynil-specific;
DE            EC=3.5.5.1;
GN   Name=bxn;
OS   Klebsiella pneumoniae subsp. ozaenae.
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=574;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=2834373; DOI=10.1016/s0021-9258(18)68787-3;
RA   Stalker D.M., Malyj L.D., McBride K.E.;
RT   "Purification and properties of a nitrilase specific for the herbicide
RT   bromoxynil and corresponding nucleotide sequence analysis of the bxn
RT   gene.";
RL   J. Biol. Chem. 263:6310-6314(1988).
CC   -!- FUNCTION: Specific for the herbicide bromoxynil (3,5-dibromo-4-
CC       hydroxybenzonitrile); converts it to its metabolite 3,5-dibromo-4-
CC       hydroxybenzoic acid.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10105};
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: Introduced by genetic manipulation and expressed in
CC       bromoxynil-tolerant cotton by Monsanto (Calgene).
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; J03196; AAA25057.1; -; Genomic_DNA.
DR   PIR; A28658; A28658.
DR   AlphaFoldDB; P10045; -.
DR   SMR; P10045; -.
DR   KEGG; ag:AAA25057; -.
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   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
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   Genetically modified food; Herbicide resistance; Hydrolase; Plasmid.
FT   CHAIN           1..349
FT                   /note="Nitrilase, bromoxynil-specific"
FT                   /id="PRO_0000204044"
FT   DOMAIN          5..274
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        161
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT                   ECO:0000255|PROSITE-ProRule:PRU10105"
SQ   SEQUENCE   349 AA;  37802 MW;  490B9A8CFD98E732 CRC64;
     MDTTFKAAAV QAEPVWMDAA ATADKTVTLV AKAAAAGAQL VAFPELWIPG YPGFMLTHNQ
     TETLPFIIKY RKQAIAADGP EIEKIRCAAQ EHNIALSFGY SERAGRTLYM SQMLIDADGI
     TKIRRRKLKP TRFERELFGE GDGSDLQVAQ TSVGRVGALN CAENLQSLNK FALAAEGEQI
     HISAWPFTLG SPVLVGDSIG AINQVYAAET GTFVLMSTQV VGPTGIAAFE IEDRYNPNQY
     LGGGYARIYG PDMQLKSKSL SPTEEGIVYA EIDLSMLEAA KYSLDPTGHY SRPDVFSVSI
     NRQRQPAVSE VIDSNGDEDP RAACEPDEGD REVVISTAIG VLPRYCGHS