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 27-MAR-2024, entry version 70.
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 GeneID; 8316291; -.
DR KEGG; pcs:Pc18g02620; -.
DR VEuPathDB; FungiDB:PCH_Pc18g02620; -.
DR eggNOG; KOG0805; Eukaryota.
DR HOGENOM; CLU_030130_6_0_1; -.
DR OMA; TSEPCWF; -.
DR OrthoDB; 2785533at2759; -.
DR BioCyc; PCHR:PC18G02620-MONOMER; -.
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; Carbon-nitrogen hydrolase; 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:SF4; CYANIDE HYDRATASE; 1.
DR PANTHER; PTHR46044; NITRILASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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
//
