ID   CHT_ALTBR               Reviewed;         363 AA.
AC   Q7Z8M6;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 49.
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=CyhAB;
OS   Alternaria brassicicola (Dark leaf spot agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Brassicicola.
OX   NCBI_TaxID=29001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=ATCC 34622;
RX   PubMed=14732258; DOI=10.1016/j.fgb.2003.10.009;
RA   Cramer R.A., Lawrence C.B.;
RT   "Identification of Alternaria brassicicola genes expressed in planta during
RT   pathogenesis of Arabidopsis thaliana.";
RL   Fungal Genet. Biol. 41:115-128(2004).
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 (By similarity). Expressed on the host leaf
CC       surface in late stages of fungal infection. {ECO:0000255|HAMAP-
CC       Rule:MF_03224, ECO:0000269|PubMed:14732258}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224}.
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DR   EMBL; AY325811; AAP88966.1; -; mRNA.
DR   AlphaFoldDB; Q7Z8M6; -.
DR   SMR; Q7Z8M6; -.
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..363
FT                   /note="Cyanide hydratase"
FT                   /id="PRO_0000440029"
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   363 AA;  40469 MW;  6D7E25334506C010 CRC64;
     MPLTKYKAAC VTSEPCWFDL EAGVQKTINF INEAGAAGCK LIAFPEVWIP GYPYWMWKIN
     YQQSLPMLKS YRENSLPMDS EEFRRIRRAA RDNQIYVSLG FSEIDHATLY LAQALIGPTG
     EVINHRRKIK PTHVEKLVYG DGAGDTFKSV TQTELGRLGQ LNCWENMNPF LKALNVSEGE
     QIHIAAWPVY PGKETLKYPD PATNVADPAS DLVTPAYAIE TGTWTLAPFQ RLSVEGLKKT
     TPEGVEPETD PSTYNGHARI YKPDGTLVCK PDKDFDGLLF VDIDLNECHL AKALADFSGH
     YMRPDLIRLL VDTRRKELIT EADTNGGIAT YTTRERLGLN IPLDAQAPKQ KATAADVPSS
     SVM