ID   CHT_FUSSL               Reviewed;         363 AA.
AC   Q96UG7;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:12000318};
DE            Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224};
DE            EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|Ref.2};
DE   AltName: Full=Cyanide-degrading nitrilase {ECO:0000255|HAMAP-Rule:MF_03224};
DE   AltName: Full=Formamide hydrolyase {ECO:0000255|HAMAP-Rule:MF_03224};
GN   Name=chy {ECO:0000303|PubMed:12000318};
OS   Fusarium solani (Filamentous fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=169388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=IMI 369371;
RX   PubMed=12000318; DOI=10.1046/j.1462-2920.2002.00284.x;
RA   Barclay M., Day J.C., Thompson I.P., Knowles C.J., Bailey M.J.;
RT   "Substrate-regulated cyanide hydratase (chy) gene expression in Fusarium
RT   solani: the potential of a transcription-based assay for monitoring the
RT   biotransformation of cyanide complexes.";
RL   Environ. Microbiol. 4:183-189(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1016/S0141-0229(98)00055-6;
RA   Barclay M., Tett V.A., Knowles C.J.;
RT   "Metabolism and enzymology of cyanide/metallocyanide biodegradation by
RT   Fusarium solani under neutral and acidic conditions.";
RL   Enzyme Microb. Technol. 23:321-330(1998).
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. Also able to transform metal cyanides.
CC       {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|Ref.2}.
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:0000255|HAMAP-Rule:MF_03224, ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.7 mM for cyanide {ECO:0000269|Ref.2};
CC         Vmax=1.7 umol/min/mg enzyme {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Oligomer of dimers, forming left-handed helical fibers.
CC       {ECO:0000255|HAMAP-Rule:MF_03224}.
CC   -!- INDUCTION: By cyanide or metal-complexed cyanide complexes
CC       K(2)Ni(CN)(4) and K(4)Fe(CN)(6). {ECO:0000269|PubMed:12000318}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224}.
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DR   EMBL; AJ310936; CAC69666.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96UG7; -.
DR   SMR; Q96UG7; -.
DR   GO; GO:0030196; F:cyanide hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000257; F:nitrilase activity; IEA:UniProt.
DR   GO; GO:0019500; P:cyanide catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07564; nitrilases_CHs; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   HAMAP; MF_03224; CN_hydrolase; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR037544; CN_hydrolase.
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; PS00921; NITRIL_CHT_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lyase.
FT   CHAIN           1..363
FT                   /note="Cyanide hydratase"
FT                   /id="PRO_0000440032"
FT   DOMAIN          6..285
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          338..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   363 AA;  40793 MW;  83EB5EC6293E5228 CRC64;
     MPITKYKAAA VTSEPGWFDL EAGVVKTIDF INEAGQAECK LVAFPEVWIP GYPYWMWKVT
     YLQSLPMLKK YRENSLTVDS EEMRRIRRAA RDNQIYVSLG FSEIDHATLY LAQVLIGPDG
     SVVNHRRKIK PTHVEKLVYG DGPGDTFMSV SETDIGRVGQ LNCWENMNPF LKALNVSCGE
     QVHIAAWPVY PGRERQVAPD PATNYADPAS DLVTPEYAIE TGAWTLAPFQ RLSVEGLKKN
     TPEGVEPETD PSVYNGHARI YRPDGSLVVK PDKDFDGLLF VDIDLNETHL TKVLADFAGH
     YMRPDLIRLL VDTRRKELIT EADPVGTIAT YTTRHRLGLD KPLDGEKKEK EATKGRDSEA
     EEL