CHT_PYRTT
ID CHT_PYRTT Reviewed; 366 AA.
AC E3RV84; A0A0P1DJ02;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=NitPt {ECO:0000303|PubMed:26521240};
GN Name=chy {ECO:0000303|PubMed:26521240};
GN Synonyms=NitPt {ECO:0000303|PubMed:26521240}; ORFNames=PTT_13066;
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557;
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=0-1;
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(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 (By similarity) (PubMed:26521240). Can also transform
CC some nitriles like 2-cyanopyridine and fumaronitrile (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; LN875502; CTQ87268.1; -; Genomic_DNA.
DR EMBL; GL535250; EFQ90364.1; -; Genomic_DNA.
DR RefSeq; XP_003301539.1; XM_003301491.1.
DR AlphaFoldDB; E3RV84; -.
DR SMR; E3RV84; -.
DR STRING; 861557.E3RV84; -.
DR EnsemblFungi; EFQ90364; EFQ90364; PTT_13066.
DR KEGG; pte:PTT_13066; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OrthoDB; 996578at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
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..366
FT /note="Cyanide hydratase"
FT /id="PRO_0000440036"
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 366 AA; 40941 MW; 6776B6406CF895FA CRC64;
MPLTKYKAAA VTSEPCWFDL TAGVQKTIDF INEAGAAGCK LVAFPEVWIP GYPYWMWKVN
YQQSLPLLKK YRENSLPIDS EEFRKIRRAA RDNQIHVSLG FSEIDHATCY LTQTLIDPTG
EVINHRRKIK PTHVEKLVYG DGAGDTFKSV TQTELGRLGQ LNCWENMNPF LKALNVSEGE
QIHIAAWPVY PGKETLNYPD PATNVAEPAS DLVTPAYAIE TGTWTLAPFQ RLSKEGLKIN
TPEGIEPETD PSTYNGHARI YRPDGSLYAK PDKDFDGLMF VDIDLNECQL TKALADFSGH
YMRPDLIRLL VDTRRKELVT EADPHGGITS YSTRQRLGLD VLLDSDVQKQ KKSGASDLGA
TNALAY
