ID   NIT_ARMGA               Reviewed;         356 AA.
AC   A0A2H3E4G0;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Cyanide hydratase {ECO:0000303|PubMed:31795104};
DE            Short=CHT {ECO:0000305};
DE            EC=4.2.1.66 {ECO:0000269|PubMed:31795104};
DE   AltName: Full=Cyanide-degrading nitrilase;
DE   AltName: Full=Formamide hydrolyase;
DE   AltName: Full=NitAg {ECO:0000303|PubMed:31795104};
GN   ORFNames=ARMGADRAFT_1007240;
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2;
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31795104; DOI=10.3390/ijms20235990;
RA   Rucka L., Chmatal M., Kulik N., Petraskova L., Pelantova H., Novotny P.,
RA   Prihodova R., Patek M., Martinkova L.;
RT   "Genetic and functional diversity of nitrilases in Agaricomycotina.";
RL   Int. J. Mol. Sci. 20:0-0(2019).
CC   -!- FUNCTION: Catalyzes the hydration of cyanide to formamide. Degradation
CC       of cyanide may be important for plant pathogenic fungi in infection of
CC       cyanogenic plants. {ECO:0000269|PubMed:31795104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formamide = H2O + hydrogen cyanide; Xref=Rhea:RHEA:21720,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16397, ChEBI:CHEBI:18407; EC=4.2.1.66;
CC         Evidence={ECO:0000269|PubMed:31795104};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ293646; PBL01211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3E4G0; -.
DR   SMR; A0A2H3E4G0; -.
DR   STRING; 47427.A0A2H3E4G0; -.
DR   EnsemblFungi; PBL01211; PBL01211; ARMGADRAFT_1007240.
DR   OMA; KIGMLNC; -.
DR   OrthoDB; 996578at2759; -.
DR   Proteomes; UP000217790; Unassembled WGS sequence.
DR   GO; GO:0030196; F:cyanide hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000257; F:nitrilase 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.
PE   1: Evidence at protein level;
KW   Hydrolase; Lyase; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Cyanide hydratase"
FT                   /id="PRO_0000451140"
FT   DOMAIN          15..290
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          331..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   356 AA;  39050 MW;  9B5D7125DF480B22 CRC64;
     MPISLNPSHS NTQTFKVAAV QAEPVWLDLQ GGVEKTIRII NEAAAEGAKI IGFPEVFIPG
     YPWTPWANNF VDAQVVLKKY QANSMPLHSP EMDRIREAVK EADVNIVLGF SERDGSSLYI
     AQVTITSDGK IANHRRKIKP THYEKTIFGD GSAQSIYNVV QTPYGRLGSL NCWEHIQPWL
     KTHFYSQYPQ IFVGGWWPAF PPHTGGSPYI VSGEASSRMS QLVSMEGGLF GIVCCHVVSE
     AGARKMRMLG FPWFTFPGGG FSVIYGPDGA ALTDPVDPGK EVVLYANISL DKIDDVKLVA
     DIMGNYSRFD LFHTTVVNGK NWKPVAYGDP DEQAASKAQQ AEIDNAGKGS IVPSKL