ID CYNS_NEOFI Reviewed; 160 AA. AC A1DIL2; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 24-JAN-2024, entry version 88. 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=NFIA_091790; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS027696; EAW19219.1; -; Genomic_DNA. DR RefSeq; XP_001261116.1; XM_001261115.1. DR AlphaFoldDB; A1DIL2; -. DR SMR; A1DIL2; -. DR STRING; 331117.A1DIL2; -. DR EnsemblFungi; EAW19219; EAW19219; NFIA_091790. DR GeneID; 4587674; -. DR KEGG; nfi:NFIA_091790; -. DR VEuPathDB; FungiDB:NFIA_091790; -. DR eggNOG; ENOG502S3YJ; Eukaryota. DR HOGENOM; CLU_103452_0_0_1; -. DR OMA; YELVMIN; -. DR OrthoDB; 2784785at2759; -. DR Proteomes; UP000006702; 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; 3.30.1160.10; Cyanate lyase, C-terminal domain; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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 NCBIfam; TIGR00673; cynS; 1. DR PANTHER; PTHR34186; CYANATE HYDRATASE; 1. DR PANTHER; PTHR34186:SF2; CYANATE HYDRATASE; 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; SSF55234; Cyanase C-terminal domain; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1. PE 3: Inferred from homology; KW Lyase; Reference proteome. FT CHAIN 1..160 FT /note="Cyanate hydratase" FT /id="PRO_0000403256" 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 160 AA; 17810 MW; 0EFC1514AEE379D9 CRC64; MSLATLDATQ HPNLPASAAT LFKAKAQNKL SFEQIAQHIG RNEVATAALF YGQAKASPED IQKLSELLNI SPQVLEEQLS GFPDRGRSVE MPPKEPLIYR LYEIVQNYGY AYKAVLNEKF GDGIMSAISF STKVEKETDA DGNNWAVITL RGKWLPFSRF //