ID   NIT1_ASPKW              Reviewed;         320 AA.
AC   G7XTA8; A0A0N7LKB9;
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=Aromatic nitrilase {ECO:0000303|PubMed:26521240};
DE            EC=3.5.5.1 {ECO:0000269|PubMed:26521240};
DE   AltName: Full=NitAk1 {ECO:0000303|PubMed:26521240};
GN   Name=nit1; ORFNames=AKAW_08281;
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 benzonitrile and 4-
CC       cyanopyridine. Also acts on dinitriles like phenylenediacetonitriles
CC       (PDAs) 1,2-PDA, 1,3-PDA, and 1,4-PDA, and cyanophenyl acetonitriles
CC       (CPAs) 2-CPA and 4-CPA, but with lower activities.
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   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; LN875495; CTQ87319.1; -; Genomic_DNA.
DR   EMBL; DF126472; GAA90167.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XTA8; -.
DR   SMR; G7XTA8; -.
DR   STRING; 40384.G7XTA8; -.
DR   VEuPathDB; FungiDB:AKAW_08281; -.
DR   eggNOG; KOG0805; Eukaryota.
DR   InParanoid; G7XTA8; -.
DR   BRENDA; 3.5.5.1; 514.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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..320
FT                   /note="Aromatic nitrilase"
FT                   /id="PRO_0000451134"
FT   DOMAIN          9..283
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   320 AA;  35987 MW;  5E26110C6172D986 CRC64;
     MSHDGPKTIR VAAVQAEPEW NNLQKGVEKT IRLIIEAGKN GANVMGFPEV WIPGYPWSIW
     NQSVVDNVEF MDEYFRNSLE RDSEEMNRIR CAVKEAGIFC VLGYSERYQG SLYISQSFID
     ENGDIVHHRR KIKPTHVERG FWGEGQADSL KSVVKSSFGN IGGLNCWEHT QTLLRYYEYA
     QNVDIHIASW PLIFGACAEM QYHISSEMCG KLTQVMSMEG ACFTLICSQV MSAENCERNK
     VDKWSFVKAP GGGFSMIYGP AGEPLVEAPD AGEEVILYAD VKLAEKWRAK QNLDVVGHYS
     RPDLLSLKVT NNAASQVHFA