CHT_STEHR
ID CHT_STEHR Reviewed; 371 AA.
AC P9WEU5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
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};
DE AltName: Full=NitSh {ECO:0000303|PubMed:31795104};
GN Name=nit; ORFNames=STEHIDRAFT_170918;
OS Stereum hirsutum (strain FP-91666) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Stereaceae; Stereum.
OX NCBI_TaxID=721885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP-91666;
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31795104; DOI=10.3390/ijms20235990;
RA Rucka L., Chmatal M., Kulik N., Petraskova L., Pelantova H., Novotny P.,
RA Prihodova R., Patek M., Martinkova L.;
RT "Genetic and functional diversity of nitrilases in Agaricomycotina.";
RL Int. J. Mol. Sci. 20:0-0(2019).
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:31795104). Also acts on 2-
CC cyanopyridine, fumaronitrile and benzonitrile, albeit at a lower rate
CC (PubMed:31795104). {ECO:0000255|HAMAP-Rule:MF_03224,
CC ECO:0000269|PubMed:31795104}.
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. {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; JH687392; EIM82695.1; -; Genomic_DNA.
DR RefSeq; XP_007307917.1; XM_007307855.1.
DR AlphaFoldDB; P9WEU5; -.
DR SMR; P9WEU5; -.
DR GeneID; 18803779; -.
DR KEGG; shs:STEHIDRAFT_170918; -.
DR OMA; GYPYWAW; -.
DR Proteomes; UP000053927; 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; 2.
DR PROSITE; PS00921; NITRIL_CHT_2; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Lyase; Reference proteome.
FT CHAIN 1..371
FT /note="Cyanide hydratase"
FT /id="PRO_0000451141"
FT DOMAIN 6..285
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT REGION 339..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 371 AA; 41428 MW; DEF08AA2D2EA9ED2 CRC64;
MPITQYKAAA VTSEPCWFDL EAGVQKTISF INEAGQAGSK LIAFPEVWIP GYPYWMWKVT
YQQSLPLLKS YRENSLPVDS EEMRRIRRAA RDNHIYVSMG FSEIDHATLY LSQVLISPTG
DVLNHRRKIK PTHVEKLVYG DGDGDTFLSV VDTDLGRLGQ LNCWENMNPF LKSLNIAMGE
QIHIAAWPVY PGKETLKYPD PATNVAEPAS DIVTPAYALE TATWTLAPFQ RLSVEGLKKN
TPAGMEPETD PSTYNGHARI YRPDGSLVVK PDKDFDGLLY VDIDLNESHL TKALGDFASG
HYMRPDLIRL LVDTRRKELV TEADPDGGVA TYSTRERLGL NRPLDPPKDE RHGIVGVAGQ
KSAEQRKAGD L
