CHT_BOTF4
ID CHT_BOTF4 Reviewed; 371 AA.
AC G2XQT1; A0A0P1DJH4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:26521240};
DE Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:26521240};
DE EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:26521240};
DE AltName: Full=Cyanide-degrading nitrilase {ECO:0000255|HAMAP-Rule:MF_03224};
DE AltName: Full=Formamide hydrolyase {ECO:0000255|HAMAP-Rule:MF_03224};
DE AltName: Full=NitBf {ECO:0000303|PubMed:26521240};
GN Name=chy {ECO:0000303|PubMed:26521240}; ORFNames=BofuT4_P068340.1;
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26521240; DOI=10.1007/s00253-015-7023-1;
RA Vesela A.B., Rucka L., Kaplan O., Pelantova H., Nesvera J., Patek M.,
RA Martinkova L.;
RT "Bringing nitrilase sequences from databases to life: the search for novel
RT substrate specificities with a focus on dinitriles.";
RL Appl. Microbiol. Biotechnol. 100:2193-2202(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 (By similarity) (PubMed:26521240). Can also transform
CC some nitriles like 2-cyanopyridine and fumaronitrile and has a minor
CC activity with 4-cyanophenyl acetonitrile (4-CPA) (PubMed:26521240).
CC {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:26521240}.
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:26521240};
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 -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224}.
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DR EMBL; LN875501; CTQ87267.1; -; Genomic_DNA.
DR EMBL; FQ790253; CCD33618.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XQT1; -.
DR SMR; G2XQT1; -.
DR STRING; 999810.G2XQT1; -.
DR EnsemblFungi; CCD33618; CCD33618; BofuT4_P068340.1.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; G2XQT1; -.
DR Proteomes; UP000008177; Unplaced contigs.
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; Reference proteome.
FT CHAIN 1..371
FT /note="Cyanide hydratase"
FT /id="PRO_0000440030"
FT DOMAIN 8..286
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 326..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 371 AA; 41446 MW; C67B4ACEA65647DF CRC64;
MPAQIKKYKA AAVQAEPGWF DLELSVKKTI HWINEAGKAG CKLVAFPEVW IPGYPYWAWK
VNYQQSLPML KAYRENSLAS DSDEMRRIRE AARENAIYVS LGYSEIDFAT LYISQVLISP
TGEVLNHRRK IKPTHVEKLV YGDGAGDTFK SVVQTDIGRV GQLNCWENMN PFLKAMNVSE
GEQVHIAGWP IYPHEETRTP LDPWTNTSNP NSDIVSPAYA IETATYVLAP FQRISKEGVD
KCTPPGVERE DHNLYNGNSR IFGPDGQCLA KADEEFEGLM FVEIDLDQSH LPKALGDFGG
HYMRPDLIRL LVDTRRKELI TEADQDGGIG TYNTQDRVGL NRPLDAPKVD GPSGVSKQVL
LSNAKKAAHK G