ID   NIT2_PENRW              Reviewed;         328 AA.
AC   B6HVR6;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Nitrilase {ECO:0000303|PubMed:23475593};
DE            EC=3.5.5.1 {ECO:0000269|PubMed:23475593};
DE   AltName: Full=NitPc2 {ECO:0000303|PubMed:23475593};
GN   ORFNames=Pc22g19330ma2m;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23475593; DOI=10.1007/s12033-013-9656-6;
RA   Kaplan O., Vesela A.B., Petrickova A., Pasquarelli F., Picmanova M.,
RA   Rinagelova A., Bhalla T.C., Patek M., Martinkova L.;
RT   "A comparative study of nitrilases identified by genome mining.";
RL   Mol. Biotechnol. 54:996-1003(2013).
CC   -!- FUNCTION: Nitrilase that hydrolyzes preferentially 4-cyanopyridine. Is
CC       also able to hydrolyze some aliphatic nitriles, such as (R,S)-
CC       mandelonitrile. {ECO:0000269|PubMed:23475593}.
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:0000269|PubMed:23475593};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; AM920437; CAP99221.1; -; Genomic_DNA.
DR   RefSeq; XP_002565836.1; XM_002565790.1.
DR   AlphaFoldDB; B6HVR6; -.
DR   SMR; B6HVR6; -.
DR   STRING; 1108849.XP_002565836.1; -.
DR   EnsemblFungi; CAP99221; CAP99221; PCH_Pc22g19330.
DR   GeneID; 8315936; -.
DR   KEGG; pcs:Pc22g19330; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g19330; -.
DR   eggNOG; KOG0805; Eukaryota.
DR   HOGENOM; CLU_030130_6_0_1; -.
DR   OMA; AFMDEYF; -.
DR   OrthoDB; 996578at2759; -.
DR   BioCyc; PCHR:PC22G19330-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
DR   GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProt.
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   Hydrolase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="Nitrilase"
FT                   /id="PRO_0000432180"
FT   DOMAIN          9..286
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   328 AA;  36809 MW;  AA68D3B2A6F1AD61 CRC64;
     MTAPVERRVR VAAIQAEPVW NDLQGGVNKV ISLLGDVGKE GANVVGFPEV FIPGYPWSIF
     TATPLDNAPF MEEYFHNSLA VDSDEMRRIQ AAVKENGTFC VLGFSERYQG SLYISQVFIN
     TDGQIVHHRR KTKPTHVERA YWGTGEGDSL KCVVDSPFGR IGGLNCWEHT QPLLRYYEYQ
     QDVDIHVASW PVLWDRPESV GSRWPYFITG DMSSRLSQVM AFEGTCFVLV CTQVMSEENF
     DKNKVRDVEH IQGTGGGFSA IFGPGGEPIA TMPSDKEGIL YANVDVNDKL RAKQWLDVVG
     HYSRPDLLSL RVNTHPSKPV FFAEEPEK