NRLA_ALCFA
ID NRLA_ALCFA Reviewed; 356 AA.
AC P20960;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Nitrilase, arylacetone-specific;
DE EC=3.5.5.1;
DE AltName: Full=Arylacetonitrilase;
OS Alcaligenes faecalis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP MUTAGENESIS OF CYS-162 AND CYS-163.
RC STRAIN=JM3;
RX PubMed=8419930; DOI=10.1073/pnas.90.1.247;
RA Kobayashi M., Izui H., Nagasawa T., Yamada H.;
RT "Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from
RT indole-3-acetonitrile: cloning of the Alcaligenes gene and site-directed
RT mutagenesis of cysteine residues.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:247-251(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-33.
RC STRAIN=JM3;
RX PubMed=2269298; DOI=10.1111/j.1432-1033.1990.tb19467.x;
RA Nagasawa T., Mauger J., Yamada H.;
RT "A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3.
RT Purification and characterization.";
RL Eur. J. Biochem. 194:765-772(1990).
CC -!- FUNCTION: Nitrilase that acts mostly on arylacetonitriles.
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: Homohexamer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; D13419; BAA02684.1; -; Genomic_DNA.
DR PIR; A47181; A47181.
DR RefSeq; WP_042484030.1; NZ_CYTB01000001.1.
DR AlphaFoldDB; P20960; -.
DR SMR; P20960; -.
DR STRING; 511.JT27_09845; -.
DR KEGG; ag:BAA02684; -.
DR eggNOG; COG0388; Bacteria.
DR BioCyc; MetaCyc:MON-11587; -.
DR BRENDA; 3.5.5.1; 232.
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.
DR PROSITE; PS00921; NITRIL_CHT_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase.
FT CHAIN 1..356
FT /note="Nitrilase, arylacetone-specific"
FT /id="PRO_0000204042"
FT DOMAIN 7..280
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 324..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 163
FT /note="Nucleophile"
FT MUTAGEN 162
FT /note="C->N: Increase of activity."
FT /evidence="ECO:0000269|PubMed:8419930"
FT MUTAGEN 163
FT /note="C->A: 100% loss of activity."
FT /evidence="ECO:0000269|PubMed:8419930"
SQ SEQUENCE 356 AA; 38908 MW; 2195465A38D40FF8 CRC64;
MQTRKIVRAA AVQAASPNYD LATGVDKTIE LARQARDEGC DLIVFGETWL PGYPFHVWLG
APAWSLKYSA RYYANSLSLD SAEFQRIAQA ARTLGIFIAL GYSERSGGSL YLGQCLIDDK
GQMLWSRRKL KPTHVERTVF GEGYARDLIV SDTELGRVGA LCCWEHLSPL SKYALYSQHE
AIHIAAWPSF SLYSEQAHAL SAKVNMAASQ IYSVEGQCFT IAASSVVTQE TLDMLEVGEH
NASLLKVGGG SSMIFAPDGR TLAPYLPHDA EGLIIADLNM EEIAFAKAIN DPVGHYSKPE
ATRLVLDLGH REPMTRVHSK SVIQEEAPEP HVQSTAAPVA VSQTQDSDTL LVQEPS