ID W7M4W3_GIBM7 Unreviewed; 356 AA.
AC W7M4W3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cyanide hydratase {ECO:0000256|ARBA:ARBA00018166, ECO:0000256|HAMAP-Rule:MF_03224};
DE Short=CHT {ECO:0000256|HAMAP-Rule:MF_03224};
DE EC=4.2.1.66 {ECO:0000256|ARBA:ARBA00013135, ECO:0000256|HAMAP-Rule:MF_03224};
DE AltName: Full=Cyanide-degrading nitrilase {ECO:0000256|HAMAP-Rule:MF_03224};
DE AltName: Full=Formamide hydrolyase {ECO:0000256|HAMAP-Rule:MF_03224};
GN ORFNames=FVEG_04370 {ECO:0000313|EMBL:EWG42610.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG42610.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG42610.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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:0000256|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:0000256|ARBA:ARBA00000092, ECO:0000256|HAMAP-
CC Rule:MF_03224};
CC -!- SUBUNIT: Oligomer of dimers, forming left-handed helical fibers.
CC {ECO:0000256|HAMAP-Rule:MF_03224}.
CC -!- INDUCTION: By cyanide. {ECO:0000256|HAMAP-Rule:MF_03224}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000256|ARBA:ARBA00008129, ECO:0000256|HAMAP-
CC Rule:MF_03224}.
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DR EMBL; DS022246; EWG42610.1; -; Genomic_DNA.
DR RefSeq; XP_018748801.1; XM_018892161.1.
DR AlphaFoldDB; W7M4W3; -.
DR STRING; 334819.W7M4W3; -.
DR EnsemblFungi; FVEG_04370T0; FVEG_04370T0; FVEG_04370.
DR GeneID; 30062443; -.
DR KEGG; fvr:FVEG_04370; -.
DR VEuPathDB; FungiDB:FVEG_04370; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OMA; TSEPCWF; -.
DR OrthoDB; 2785533at2759; -.
DR Proteomes; UP000009096; Chromosome 4.
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; Carbon-nitrogen hydrolase; 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:SF4; CYANIDE HYDRATASE; 1.
DR PANTHER; PTHR46044; NITRILASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03224};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 6..285
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT ACT_SITE 46
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10139"
SQ SEQUENCE 356 AA; 39926 MW; 3717A39968BF7BBC CRC64;
MAITKYKAAA VTSEPGWFDL EGGVRKTIDF INEAGQAGCK LVAFPEVWIP GYPYWMWKVT
YLQSLPMLKR YRENSMAVDS EEMRRIRRAA RDNQIYVSLG FSEIDHATLY LAQVLIGPDG
SVINHRRKIK PTHVEKLVYG DGSGDTFMAV SETDIGRVGQ LNCWENMNPF LKSLNVSAGE
QVHIAAWPVY PGKERQVAPD PATNYADPAS DLVTPEYAIE TGTWTLAPFQ RLSVEGLKIN
TPEGVEPETD PSVYNGHARI YRPDGSLVVK PEKDFDGLLF VDIDLNETHL TKVLADFAGH
YMRPDLIRLL VDTRRKELIT EADANGSIAT YTTRQRLGLD KPLDDKKGEH ETPEVV
//
