ID G2XEY0_VERDV Unreviewed; 361 AA.
AC G2XEY0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=VDAG_08712 {ECO:0000313|EMBL:EGY18378.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY18378.1};
RN [1] {ECO:0000313|EMBL:EGY18378.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18378.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS572716; EGY18378.1; -; Genomic_DNA.
DR RefSeq; XP_009649324.1; XM_009651029.1.
DR AlphaFoldDB; G2XEY0; -.
DR SMR; G2XEY0; -.
DR STRING; 498257.G2XEY0; -.
DR EnsemblFungi; EGY18378; EGY18378; VDAG_08712.
DR GeneID; 20710175; -.
DR KEGG; vda:VDAG_08712; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; G2XEY0; -.
DR OMA; TSEPCWF; -.
DR OrthoDB; 2785533at2759; -.
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}.
FT DOMAIN 1..279
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 335..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10139"
SQ SEQUENCE 361 AA; 40320 MW; 3A0679A19A5E1B4C CRC64;
MPITKYKAAA WFDLEAGVQK TINFINEAGQ AGCKLVAFPE VWIPGYPYWM WKVTYLQSLP
MLKRYRENSL RVDSEEMRRI RRAARANQVF VSMGFSELDH ATLYLAQVLI TPTGAIANHR
RKIKPTHVEK LVYGDGAGDT FASVVETEIG RVGQLNCWEN MNPFLKALNV SMGEQVHVAA
WPVYPGKERR VAPDPATNYA DPASDLVTPA YAMETGAWVL APFQRLSVEG LRVNTPEGVE
PETDPSVYNG HARIYRPDGS LVVKPEKDFD GLLFVDIDLN ETHLTKVLAD FAGHYMRPDL
IRLLVDTRRK ELVTEAEGQN GIVSYSTAHR LGLDRPLDSV PERDAKKVGG NEAALKSVHE
G
//
