ID   CYNS_PARBP              Reviewed;         163 AA.
AC   C0S4M2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=PABG_02627;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN305533; EEH20368.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0S4M2; -.
DR   SMR; C0S4M2; -.
DR   EnsemblFungi; EEH20368; EEH20368; PABG_02627.
DR   VEuPathDB; FungiDB:PABG_02627; -.
DR   HOGENOM; CLU_103452_0_0_1; -.
DR   InParanoid; C0S4M2; -.
DR   Proteomes; UP000002740; 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   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   Gene3D; 3.30.1160.10; -; 1.
DR   HAMAP; MF_00535; Cyanate_hydrat; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
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.
FT   CHAIN           1..163
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_0000403259"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03139"
SQ   SEQUENCE   163 AA;  18121 MW;  15278F37A831803C CRC64;
     MSNINLATLD ISEHPNLPSS SAVLFEAKAR KKLSFEAIAS AIGRNEVATA AIFYGQAKAS
     AEDIVKLSEV LGIDHLYLES LLSGFPDRGK SMTFPPKDPL IYRLFEIVQN YGYAYKAVMN
     EKFGDGIMSA ISFSTKVEKE TDLDGNNWAV VTWRGKWLPY SRF