ID   NIT2_ASPKW              Reviewed;         328 AA.
AC   G7X8S6; A0A0P1DJB4;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Arylacetonitrilase {ECO:0000303|PubMed:26521240};
DE            EC=3.5.5.1 {ECO:0000269|PubMed:26521240};
DE            EC=3.5.5.5 {ECO:0000269|PubMed:26521240};
DE   AltName: Full=NitAk2 {ECO:0000303|PubMed:26521240};
GN   Name=nit2; ORFNames=AKAW_01332 {ECO:0000312|EMBL:GAA83217.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=26521240; DOI=10.1007/s00253-015-7023-1;
RA   Vesela A.B., Rucka L., Kaplan O., Pelantova H., Nesvera J., Patek M.,
RA   Martinkova L.;
RT   "Bringing nitrilase sequences from databases to life: the search for novel
RT   substrate specificities with a focus on dinitriles.";
RL   Appl. Microbiol. Biotechnol. 100:2193-2202(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile
CC       and (R,S)-mandelonitrile. Also acts on dinitriles like
CC       phenylenediacetonitriles (PDAs) 1,2-PDA, 1,3-PDA, and 1,4-PDA, and
CC       cyanophenyl acetonitriles (CPAs) 2-CPA and 4-CPA.
CC       {ECO:0000269|PubMed:26521240}.
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:26521240};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate +
CC         NH4(+); Xref=Rhea:RHEA:20657, ChEBI:CHEBI:15377, ChEBI:CHEBI:16237,
CC         ChEBI:CHEBI:17346, ChEBI:CHEBI:28938; EC=3.5.5.5;
CC         Evidence={ECO:0000269|PubMed:26521240};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; LN875496; CTQ87320.1; -; Genomic_DNA.
DR   EMBL; DF126449; GAA83217.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7X8S6; -.
DR   SMR; G7X8S6; -.
DR   STRING; 40384.G7X8S6; -.
DR   VEuPathDB; FungiDB:AKAW_01332; -.
DR   eggNOG; KOG0805; Eukaryota.
DR   InParanoid; G7X8S6; -.
DR   BRENDA; 3.5.5.5; 514.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0047428; F:arylacetonitrilase activity; IEA:UniProtKB-EC.
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.
FT   CHAIN           1..328
FT                   /note="Arylacetonitrilase"
FT                   /id="PRO_0000451135"
FT   DOMAIN          5..278
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        160
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   328 AA;  35821 MW;  57E78101FBAE586C CRC64;
     MSSQVRVAVT QAEPVWLDLD ATVKKTCDLI VEAAANGAQL VAFPECWIPG YPAWIWTRPV
     DMRLSSTYIQ NSLKIDSPQM ASIQKCAAEN KIVVVLGFSE NLHNSLYISQ AIIGSDGKIL
     TTRKKIKPTH MERTIFGDSF GDCLQSVVDT SAGRVGALSC WEHIQPLLKY HTYAQREQIH
     VAAWPPLFPH NEDGSLFSMS SEGTSSIART YAIESQSFVL HTTTVIGQSG VDRMATHGGA
     LMSTPGGGCS AIFGPDGRQL SQPIPSTEEG IIYADLDLDQ IYHSKAFVDV CGHYSRPDLL
     WLGVEGSVKR HVRENAATVA AEAEQQEQ