ID   CYNS_ASPCL              Reviewed;         154 AA.
AC   A1C7Y5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Cyanate hydratase {ECO:0000255|HAMAP-Rule:MF_03139};
DE            Short=Cyanase {ECO:0000255|HAMAP-Rule:MF_03139};
DE            EC=4.2.1.104 {ECO:0000255|HAMAP-Rule:MF_03139};
DE   AltName: Full=Cyanate hydrolase {ECO:0000255|HAMAP-Rule:MF_03139};
DE   AltName: Full=Cyanate lyase {ECO:0000255|HAMAP-Rule:MF_03139};
GN   Name=cyn1 {ECO:0000255|HAMAP-Rule:MF_03139}; ORFNames=ACLA_075450;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC       ammonia and carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_03139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+);
CC         Xref=Rhea:RHEA:11120, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:29195;
CC         EC=4.2.1.104; Evidence={ECO:0000255|HAMAP-Rule:MF_03139};
CC   -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03139}.
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DR   EMBL; DS027045; EAW14506.1; -; Genomic_DNA.
DR   RefSeq; XP_001275932.1; XM_001275931.1.
DR   AlphaFoldDB; A1C7Y5; -.
DR   SMR; A1C7Y5; -.
DR   STRING; 5057.CADACLAP00006299; -.
DR   EnsemblFungi; EAW14506; EAW14506; ACLA_075450.
DR   GeneID; 4707675; -.
DR   KEGG; act:ACLA_075450; -.
DR   VEuPathDB; FungiDB:ACLA_075450; -.
DR   eggNOG; ENOG502S3YJ; Eukaryota.
DR   HOGENOM; CLU_103452_0_0_1; -.
DR   OMA; YELVMIN; -.
DR   OrthoDB; 1486663at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0008824; F:cyanate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009439; P:cyanate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00559; Cyanase_C; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   Gene3D; 3.30.1160.10; -; 1.
DR   HAMAP; MF_00535; Cyanate_hydrat; 1.
DR   InterPro; IPR008076; Cyanase.
DR   InterPro; IPR003712; Cyanate_lyase_C.
DR   InterPro; IPR036581; Cyanate_lyase_C_sf.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   PANTHER; PTHR34186; PTHR34186; 1.
DR   Pfam; PF02560; Cyanate_lyase; 1.
DR   PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR   PRINTS; PR01693; CYANASE.
DR   SMART; SM01116; Cyanate_lyase; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF55234; SSF55234; 1.
DR   TIGRFAMs; TIGR00673; cynS; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..154
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_0000403239"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ   SEQUENCE   154 AA;  17035 MW;  814A2103C67FE767 CRC64;
     MSLATLDATQ HPNLPQSSQT LFSAKATKKL TFEQIAQHIG RNEVAAAAIF YGQAKASPED
     IEKLSSLLDI PTPVLEEQLG GFPDRGRSVE MPPKEPLIYR LYEIVQNYGY AYKAVLNEKF
     GDGIMSAISF STKVEKETDA DGNNWAVITL RGKW