ID   NRL2_RHORH              Reviewed;         366 AA.
AC   Q03217;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Aliphatic nitrilase;
DE            EC=3.5.5.7;
GN   Name=nitA;
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-165.
RC   STRAIN=J1;
RX   PubMed=1400390; DOI=10.1016/s0021-9258(19)36749-3;
RA   Kobayashi M., Komeda H., Yanaka N., Nagasawa T., Yamada H.;
RT   "Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression
RT   of the gene and identification of an essential cysteine residue.";
RL   J. Biol. Chem. 267:20746-20751(1992).
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; D11425; BAA01994.1; -; Genomic_DNA.
DR   EMBL; D67026; BAA11037.1; -; Genomic_DNA.
DR   PIR; A45070; A45070.
DR   AlphaFoldDB; Q03217; -.
DR   SMR; Q03217; -.
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   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..366
FT                   /note="Aliphatic nitrilase"
FT                   /id="PRO_0000204046"
FT   DOMAIN          8..282
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          346..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT                   ECO:0000255|PROSITE-ProRule:PRU10105"
FT   MUTAGEN         165
FT                   /note="C->S,A: 100% loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1400390"
SQ   SEQUENCE   366 AA;  40189 MW;  3B8E1274AE5EC287 CRC64;
     MVEYTNTFKV AAVQAQPVWF DAAKTVDKTV SIIAEAARNG CELVAFPEVF IPGYPYHIWV
     DSPLAGMAKF AVRYHENSLT MDSPHVQRLL DAARDHNIAV VVGISERDGG SLYMTQLVID
     ADGQLVARRR KLKPTHVERS VYGEGNGSDI SVYDMPFARL GALNCWEHFQ TLTKYAMYSM
     HEQVHVASWP GMSLYQPEVP AFGVDAQLTA TRMYALEGQT FVVCTTQVVT PEAHEFFCDN
     DEQRKLIGRG GGFARIIGPD GRDLATPLAE DEEGILYADI DLSAITLAKQ AADPVGHYSR
     PDVLSLNFNQ RHTTPVNTAI STIHATHTLV PQSGALDGVR ELNGADEQRA LPSTHSDETD
     RATASI