CHT_NEUCR
ID CHT_NEUCR Reviewed; 351 AA.
AC Q7RVT0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:18587571};
DE Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:18587571};
DE EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:18587571};
DE AltName: Full=Cyanide-degrading nitrilase {ECO:0000255|HAMAP-Rule:MF_03224};
DE AltName: Full=Formamide hydrolyase {ECO:0000255|HAMAP-Rule:MF_03224};
GN Name=cnh-1 {ECO:0000303|PubMed:18946669};
GN Synonyms=cht {ECO:0000303|PubMed:18587571}; ORFNames=NCU04697;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=18587571; DOI=10.1007/s00253-008-1559-2;
RA Basile L.J., Willson R.C., Sewell B.T., Benedik M.J.;
RT "Genome mining of cyanide-degrading nitrilases from filamentous fungi.";
RL Appl. Microbiol. Biotechnol. 80:427-435(2008).
RN [3]
RP SUBUNIT.
RX PubMed=18946669; DOI=10.1007/s00253-008-1735-4;
RA Dent K.C., Weber B.W., Benedik M.J., Sewell B.T.;
RT "The cyanide hydratase from Neurospora crassa forms a helix which has a
RT dimeric repeat.";
RL Appl. Microbiol. Biotechnol. 82:271-278(2009).
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:0000255|HAMAP-Rule:MF_03224,
CC ECO:0000269|PubMed:18587571}.
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:18587571};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7. Active fom pH 5 to pH 9.
CC {ECO:0000269|PubMed:18587571};
CC -!- SUBUNIT: Oligomer of dimers, forming left-handed helical fibers with a
CC diameter of 13 nm but with lengths ranging from approximately 1 um at
CC the leading edge of the peak to having approximately the same length
CC and diameter at the trailing edge. {ECO:0000255|HAMAP-Rule:MF_03224,
CC ECO:0000269|PubMed:18946669}.
CC -!- INDUCTION: By cyanide. {ECO:0000255|HAMAP-Rule:MF_03224,
CC ECO:0000269|PubMed:18587571}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000255|HAMAP-Rule:MF_03224}.
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DR EMBL; CM002241; EAA30924.2; -; Genomic_DNA.
DR RefSeq; XP_960160.2; XM_955067.3.
DR AlphaFoldDB; Q7RVT0; -.
DR SMR; Q7RVT0; -.
DR STRING; 5141.EFNCRP00000004519; -.
DR EnsemblFungi; EAA30924; EAA30924; NCU04697.
DR GeneID; 3876307; -.
DR KEGG; ncr:NCU04697; -.
DR VEuPathDB; FungiDB:NCU04697; -.
DR HOGENOM; CLU_030130_6_0_1; -.
DR InParanoid; Q7RVT0; -.
DR OMA; GYPYWAW; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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..351
FT /note="Cyanide hydratase"
FT /id="PRO_0000440035"
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 351 AA; 39526 MW; 52355FCBD1F134BA CRC64;
MVLTKYKAAA VTSEPCWFDL EGGVRKTIDF INEAGQAGCK LVAFPEVWIP GYPYWMWKVT
YQQSLPMLKK YRENAMAVDS DEFRRIRRAA RDNQIYVSLG FAEIDHATLY LAQALIDPTG
EVINHRRKIK PTHVEKLVYG DGAGDTFMSV TPTELGRLGQ LNCWENMNPF LKSLNVSMGE
QIHIAAWPIY PGKETLKYPD PATNVADPAS DLVTPAYAIE TGTWTLAPFQ RLSVEGLKKN
TPEGVEPETD PSTYNGHARI YRPDGSLVVR PDKDFDGLLF VDIDLNECHL TKALADFAGH
YMRPDLIRLL VDTSRKELVT EVDRNGGIVQ YSTRERLGLN TPLENDKEGK K
