ID   CHT_GIBBA               Reviewed;         355 AA.
AC   P32963;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:8409923};
DE            Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224};
DE            EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:8409923};
DE   AltName: Full=Cyanide-degrading nitrilase {ECO:0000255|HAMAP-Rule:MF_03224};
DE   AltName: Full=Formamide hydrolyase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:8409923};
GN   Name=chy1 {ECO:0000303|PubMed:8409923};
OS   Gibberella baccata (Fusarium lateritium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium lateritium species complex.
OX   NCBI_TaxID=5523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=IMI 300533;
RX   PubMed=8409923; DOI=10.1099/00221287-139-8-1807;
RA   Cluness M.J., Turner P.D., Clements E., Brown D.T., O'Reilly C.;
RT   "Purification and properties of cyanide hydratase from Fusarium lateritium
RT   and analysis of the corresponding chy1 gene.";
RL   J. Gen. Microbiol. 139:1807-1815(1993).
RN   [2]
RP   MUTAGENESIS OF CYS-163.
RX   PubMed=8586260; DOI=10.1111/j.1574-6968.1995.tb07928.x;
RA   Brown D.T., Turner P.D., O'Reilly C.;
RT   "Expression of the cyanide hydratase enzyme from Fusarium lateritium in
RT   Escherichia coli and identification of an essential cysteine residue.";
RL   FEMS Microbiol. Lett. 134:143-146(1995).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF PHE-170.
RX   PubMed=12725921; DOI=10.1016/s0378-1097(03)00170-8;
RA   Nolan L.M., Harnedy P.A., Turner P., Hearne A.B., O'Reilly C.;
RT   "The cyanide hydratase enzyme of Fusarium lateritium also has nitrilase
RT   activity.";
RL   FEMS Microbiol. Lett. 221:161-165(2003).
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 (PubMed:8409923). Has also low but significant
CC       nitrilase activity with acetonitrile, propionitrile and benzonitrile
CC       (PubMed:12725921). {ECO:0000255|HAMAP-Rule:MF_03224,
CC       ECO:0000269|PubMed:12725921, ECO:0000269|PubMed:8409923}.
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,
CC         ECO:0000269|PubMed:8409923};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=43 mM for cyanide {ECO:0000269|PubMed:8409923};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:8409923};
CC   -!- SUBUNIT: Oligomer of dimers, forming left-handed helical fibers.
CC       {ECO:0000255|HAMAP-Rule:MF_03224}.
CC   -!- INDUCTION: By cyanide. {ECO:0000255|HAMAP-Rule:MF_03224,
CC       ECO:0000269|PubMed:8409923}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33336.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M99046; AAA33336.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; P32963; -.
DR   SMR; P32963; -.
DR   BRENDA; 4.2.1.66; 2350.
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; PS00920; NITRIL_CHT_1; 1.
DR   PROSITE; PS00921; NITRIL_CHT_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lyase.
FT   CHAIN           1..355
FT                   /note="Cyanide hydratase"
FT                   /id="PRO_0000204047"
FT   DOMAIN          6..286
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT   MUTAGEN         163
FT                   /note="C->A: Completely abolishes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:8586260"
FT   MUTAGEN         170
FT                   /note="F->L: Completely abolishes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:12725921"
SQ   SEQUENCE   355 AA;  39879 MW;  B6304651F5360B5D CRC64;
     MAITKYKAAA VTSEPGWFDL EGGVRKTIDF INEAGEAGCK FVAFPEVWIP GYPYWMWKVT
     YLQSLPMLKR YRENSMAVDS EEMRRIRRAA RDNQIFVSLG FSEIDHATLY LSQVLIGPDG
     AVINHRRKIK PTHVEKLVYG DGSGDTFMSV SETEIGRVGQ LNCWENMNPF LKSLNVSAGE
     QVHVAAWPVY PGKERQVHPD PATNYADPAS DLVTPEYAIE TGTWTLAPFQ RLSVEGLKIN
     TPEGVEPETD PSVYNGHARI YRPDGSLVVK PEKDFDGLLF VDIDLNECHL TKVLADFAGH
     YMRPDLIRLL VDTRRKKLIT EADPNGSIAT YSTRQRLGLD KPLSKKEGDE TTDVL