ID   CHT_PENRW               Reviewed;         358 AA.
AC   B6HCY4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cyanide hydratase {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000303|PubMed:23475593};
DE            Short=CHT {ECO:0000255|HAMAP-Rule:MF_03224};
DE            EC=4.2.1.66 {ECO:0000255|HAMAP-Rule:MF_03224, ECO:0000269|PubMed:23475593};
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=NitPc1 {ECO:0000303|PubMed:23475593};
GN   ORFNames=PCH_Pc18g02620;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23475593; DOI=10.1007/s12033-013-9656-6;
RA   Kaplan O., Vesela A.B., Petrickova A., Pasquarelli F., Picmanova M.,
RA   Rinagelova A., Bhalla T.C., Patek M., Martinkova L.;
RT   "A comparative study of nitrilases identified by genome mining.";
RL   Mol. Biotechnol. 54:996-1003(2013).
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:23475593}.
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:23475593};
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, ECO:0000305}.
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DR   EMBL; AM920433; CAP94486.1; -; Genomic_DNA.
DR   RefSeq; XP_002562104.1; XM_002562058.1.
DR   AlphaFoldDB; B6HCY4; -.
DR   SMR; B6HCY4; -.
DR   STRING; 500485.B6HCY4; -.
DR   EnsemblFungi; CAP94486; CAP94486; PCH_Pc18g02620.
DR   GeneID; 8316291; -.
DR   KEGG; pcs:Pc18g02620; -.
DR   VEuPathDB; FungiDB:PCH_Pc18g02620; -.
DR   eggNOG; KOG0805; Eukaryota.
DR   HOGENOM; CLU_030130_6_0_1; -.
DR   OMA; GYPYWAW; -.
DR   OrthoDB; 996578at2759; -.
DR   BioCyc; PCHR:PC18G02620-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c18.
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.
PE   1: Evidence at protein level;
KW   Hydrolase; Lyase; Reference proteome.
FT   CHAIN           1..358
FT                   /note="Cyanide hydratase"
FT                   /id="PRO_0000432181"
FT   DOMAIN          8..287
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
FT   ACT_SITE        165
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03224"
SQ   SEQUENCE   358 AA;  39966 MW;  7BCD54631BEBDC2E CRC64;
     MVPVLKKYKA AAVNAEPGWF DLQESVRRTI HWIDEAGKAG CKLIAFPELW IPGYPYWAWK
     VNYQESLPLL KKYRENSLPS DSDEMRRIRE AAKANKIWVS LGYSELDLAS LYTTQIMISP
     AGDVINHRRK IKATHVERLV FGDGTGDTTE SVMDTEIGRI GHLNCWENMN PFLKAYAASL
     GEQVHIAAWP LYPGKETLKY PDPYTNVAEA NADLVTPAYA IETGSFTLAP WQTITAEGIK
     LNTPPGKELE DPNIYNGNGR IFGPDGQNLV PHPDKDFQGL LFVDIDLDEI HLTKSLADFG
     GHYMRPDLIR LLVDTNRKDL VVHEDRVNGG VAYTRTIDRV GLSAPLDASA TEAQSESV