NITR1_BRADU
ID NITR1_BRADU Reviewed; 334 AA.
AC Q89GE3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Nitrilase bll6402;
DE EC=3.5.5.1;
DE AltName: Full=Mandelonitrile hydrolase;
GN OrderedLocusNames=bll6402;
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=17350705; DOI=10.1016/j.jbiotec.2007.02.001;
RA Zhu D., Mukherjee C., Biehl E.R., Hua L.;
RT "Discovery of a mandelonitrile hydrolase from Bradyrhizobium japonicum
RT USDA110 by rational genome mining.";
RL J. Biotechnol. 129:645-650(2007).
RN [3]
RP FUNCTION.
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 mediates the hydrolysis of aromatic alpha-
CC hydroxy nitriles to carboxylic acids. Has high activity toward
CC mandelonitrile and mediates its hydrolysis to mandelic acid. Also
CC mediates hydrolysis of mandelonitrile derivatives. Has weak activity
CC toward aliphatic nitriles. {ECO:0000269|PubMed:17350705,
CC ECO:0000269|PubMed:18061298}.
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 ECO:0000269|PubMed:17350705};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for mandelonitrile {ECO:0000269|PubMed:17350705};
CC Note=kcat is 27.0 sec(-1) with mandelonitrile.;
CC -!- SUBUNIT: Homomultimer composed of 12 subunits.
CC {ECO:0000269|PubMed:17350705}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; BA000040; BAC51667.1; -; Genomic_DNA.
DR RefSeq; NP_773042.1; NC_004463.1.
DR RefSeq; WP_011089142.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89GE3; -.
DR SMR; Q89GE3; -.
DR STRING; 224911.27354681; -.
DR EnsemblBacteria; BAC51667; BAC51667; BAC51667.
DR GeneID; 64026160; -.
DR KEGG; bja:bll6402; -.
DR PATRIC; fig|224911.44.peg.6385; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_030130_6_0_5; -.
DR InParanoid; Q89GE3; -.
DR OMA; WPSFSLY; -.
DR PhylomeDB; Q89GE3; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR GO; GO:0000257; F:nitrilase activity; IDA:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:UniProtKB.
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..334
FT /note="Nitrilase bll6402"
FT /id="PRO_0000422216"
FT DOMAIN 6..284
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 46
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,
FT ECO:0000255|PROSITE-ProRule:PRU10105"
SQ SEQUENCE 334 AA; 36203 MW; 292C9564FE840C20 CRC64;
MQDTKFKVAV VQAAPVFMDA PASVAKAIGF IAEAGAAGAK LLAFPEVWIP GYPWWLWLGT
PAWGMQFVPR YHANSLRADG PDILALCAAA AEAKINVVMG FSEIDGGTLY LSQVFISDAG
EIIFKRRKLK PTHVERTLYG EGDGSDFRVV ESSVGRLGAL CCAEHIQPLS KYAMYSMNEQ
VHVASWPSFT LYRDKAYALG HEVNLAASQI YALEGGCFVL HASAITGQDM FDMLCDTPEK
ADLLNAEGAK PGGGYSMIFG PDGQPMCEHL PQDKEGILYA DVDLSMIAIA KAAYDPTGHY
ARGDVVRLMV NRSPRRTSVS FSEDENAAVT FTET
