CHT_MICSH
ID CHT_MICSH Reviewed; 368 AA.
AC P32964;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:1416986};
DE Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:1416986};
DE EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:1416986};
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=cht {ECO:0000303|PubMed:15703908};
OS Microdochium sorghi (Zonate leaf spot disease fungus) (Gloeocercospora
OS sorghi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=1682391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-442;
RX PubMed=1382413; DOI=10.1016/0006-291x(92)91303-8;
RA Wang P., van Etten H.D.;
RT "Cloning and properties of a cyanide hydratase gene from the
RT phytopathogenic fungus Gloeocercospora sorghi.";
RL Biochem. Biophys. Res. Commun. 187:1048-1054(1992).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=T-442;
RX PubMed=1416986; DOI=10.1016/0003-9861(92)90451-2;
RA Wang P., Matthews D.E., VanEtten H.D.;
RT "Purification and characterization of cyanide hydratase from the
RT phytopathogenic fungus Gloeocercospora sorghi.";
RL Arch. Biochem. Biophys. 298:569-575(1992).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=T-442;
RX PubMed=10587474; DOI=10.1006/fgbi.1999.1167;
RA Wang P., Sandrock R.W., VanEtten H.D.;
RT "Disruption of the cyanide hydratase gene in Gloeocercospora sorghi
RT increases its sensitivity to the phytoanticipin cyanide but does not affect
RT its pathogenicity on the cyanogenic plant sorghum.";
RL Fungal Genet. Biol. 28:126-134(1999).
RN [4]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15703908; DOI=10.1007/s00253-005-1903-8;
RA Jandhyala D.M., Willson R.C., Sewell B.T., Benedik M.J.;
RT "Comparison of cyanide-degrading nitrilases.";
RL Appl. Microbiol. Biotechnol. 68:327-335(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18587571; DOI=10.1007/s00253-008-1559-2;
RA Basile L.J., Willson R.C., Sewell B.T., Benedik M.J.;
RT "Genome mining of cyanide-degrading nitrilases from filamentous fungi.";
RL Appl. Microbiol. Biotechnol. 80:427-435(2008).
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:0000255|HAMAP-Rule:MF_03224,
CC ECO:0000269|PubMed:1416986}.
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:1416986};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 mM for cyanide (at pH 8 and 25 degrees Celsium)
CC {ECO:0000269|PubMed:1416986};
CC KM=90 mM for cyanide (at pH 7.8 and 23 degrees Celsium)
CC {ECO:0000269|PubMed:15703908};
CC Vmax=4.4 mmol/min/mg enzyme {ECO:0000269|PubMed:15703908};
CC pH dependence:
CC Optimum pH is 7-8 (PubMed:1416986, PubMed:15703908). Active from pH 6
CC to pH 8.5 (PubMed:15703908, PubMed:18587571).
CC {ECO:0000269|PubMed:1416986, ECO:0000269|PubMed:15703908,
CC ECO:0000269|PubMed:18587571};
CC Temperature dependence:
CC Optimum temperature is 42-55 degrees Celsius.
CC {ECO:0000269|PubMed:15703908};
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 -!- DISRUPTION PHENOTYPE: Highly sensitive to cyanide, but retains
CC virulence on sorghum. {ECO:0000269|PubMed:10587474}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000305}.
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DR EMBL; M99044; AAA33353.1; -; Genomic_DNA.
DR PIR; JQ1613; JQ1613.
DR AlphaFoldDB; P32964; -.
DR SMR; P32964; -.
DR BioCyc; MetaCyc:MON-17777; -.
DR BRENDA; 4.2.1.66; 2449.
DR PHI-base; PHI:143; -.
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..368
FT /note="Cyanide hydratase"
FT /id="PRO_0000204048"
FT DOMAIN 6..285
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 341..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 368 AA; 40899 MW; 5A03113E515A3575 CRC64;
MPINKYKAAV VTSEPVWENL EGGVVKTIEF INEAGKAGCK LIAFPEVWIP GYPYWMWKVN
YLQSLPMLKA YRENSIAMDS SEMRRIRAAA RDNQIYVSIG VSEIDHATLY LTQVLISPLG
DVINHRRKIK PTHVEKLVYG DGSGDSFEPV TQTEIGRLGQ LNCWENMNPF LKSLAVARGE
QIHVAAWPVY PDLSKQVHPD PATNYADPAS DLVTPAYAIE TGTWVLAPFQ RISVEGLKRH
TPPGVEPETD ATPYNGHARI FRPDGSLYAK PAVDFDGLMY VDIDLNESHL TKALADFAGH
YMRPDLIRLL VDTRRKELVT EVGGGDNGGI QSYSTMARLG LDRPLEEEDY RQGTDAGETE
KASSNGHA
