CHT_LEPMC
ID CHT_LEPMC Reviewed; 356 AA.
AC Q9P8V3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224};
DE Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224};
DE EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224};
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:10821180};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=M1;
RX PubMed=10821180; DOI=10.1007/s004380051190;
RA Sexton A.C., Howlett B.J.;
RT "Characterisation of a cyanide hydratase gene in the phytopathogenic fungus
RT Leptosphaeria maculans.";
RL Mol. Gen. Genet. 263:463-470(2000).
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 -!- 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 -!- SUBUNIT: Oligomer of dimers, forming left-handed helical fibers.
CC {ECO:0000255|HAMAP-Rule:MF_03224}.
CC -!- INDUCTION: By cyanide and propionitrile. {ECO:0000269|PubMed:10821180}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224}.
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DR EMBL; AF192405; AAF66098.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P8V3; -.
DR SMR; Q9P8V3; -.
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 2: Evidence at transcript level;
KW Hydrolase; Lyase.
FT CHAIN 1..356
FT /note="Cyanide hydratase"
FT /id="PRO_0000440034"
FT DOMAIN 6..285
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
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 356 AA; 39774 MW; 9A322850BB3DFFB2 CRC64;
MPLTKYKAAA VTSEPAWFNL EAGVQKTIDF INEAGQAGCK LIAFPEVWIP GYPYWMWKIN
YQQSLPMLKK YRENSMAVDS DEFRRIRRAA RDNQIHVSLG FSEIDHATLY LAQALISPTG
EVLNHRRKIK PTHVEKLVYG DGAGDTFTSV VPTELGRLGQ LNCWENMNPF LKALNVSAGE
QIHIAAWPVY PGKETLKYPD PATNVADPAS DLVTPAYAIE TGTWTLAPFQ RLSAEGLKMN
TPEGVEPETD PTTYNGHARI YRPDGSLVVK PDKDFDGLLF VDIDLNECHL TKALADFSGH
YMRPDLIRLL VDTRRKELVT EAEGNDGVKA YSTRERLGLN LPLDGSKEDE KVPVAL
