ID   NRL1_RHORH              Reviewed;         383 AA.
AC   Q02068;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Aliphatic nitrilase;
DE            EC=3.5.5.7;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   MUTAGENESIS OF CYS-170.
RC   STRAIN=K22;
RX   PubMed=1390687; DOI=10.1021/bi00152a042;
RA   Kobayashi M., Yanaka N., Nagasawa T., Yamada H.;
RT   "Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic
RT   nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and
RT   identification of its active site residue.";
RL   Biochemistry 31:9000-9007(1992).
CC   -!- FUNCTION: Acts on aliphatic nitriles such as acrylonitrile,
CC       crotononitrile and glutaronitrile.
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   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; D12583; BAA02127.1; -; Genomic_DNA.
DR   PIR; A43470; A43470.
DR   AlphaFoldDB; Q02068; -.
DR   SMR; Q02068; -.
DR   KEGG; ag:BAA02127; -.
DR   BRENDA; 3.5.5.7; 5395.
DR   GO; GO:0018762; F:aliphatic 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..383
FT                   /note="Aliphatic nitrilase"
FT                   /id="PRO_0000204045"
FT   DOMAIN          13..288
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          359..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT                   ECO:0000255|PROSITE-ProRule:PRU10105"
FT   MUTAGEN         170
FT                   /note="C->S,A: 100% loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1390687"
SQ   SEQUENCE   383 AA;  42276 MW;  BA8EE5572B8DA17B CRC64;
     MSSNPELKYT GKVKVATVQA EPVILDADAT IDKAIGFIEE AAKNGAEFLA FPEVWIPGYP
     YWAWIGDVKW AVSDFIPKYH ENSLTLGDDR MRRLQLAARQ NNIALVMGYS EKDGASRYLS
     QVFIDQNGDI VANRRKLKPT HVERTIYGEG NGTDFLTHDF GFGRVGGLNC WEHFQPLSKY
     MMYSLNEQIH VASWPAMFAL TPDVHQLSVE ANDTVTRSYA IEGQTFVLAS THVIGKATQD
     LFAGDDDAKR ALLPLGQGWA RIYGPDGKSL AEPLPEDAEG LLYAELDLEQ IILAKAAADP
     AGHYSRPDVL SLKIDTRNHT PVQYITADGR TSLNSNSRVE NYRLHQLADI EKYENAEAAT
     LPLDAPAPAP APEQKSGRAK AEA