CYNS_CUPNH
ID CYNS_CUPNH Reviewed; 147 AA.
AC Q0K572;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Cyanate hydratase {ECO:0000255|HAMAP-Rule:MF_00535};
DE Short=Cyanase {ECO:0000255|HAMAP-Rule:MF_00535};
DE EC=4.2.1.104 {ECO:0000255|HAMAP-Rule:MF_00535};
DE AltName: Full=Cyanate hydrolase {ECO:0000255|HAMAP-Rule:MF_00535};
DE AltName: Full=Cyanate lyase {ECO:0000255|HAMAP-Rule:MF_00535};
GN Name=cynS {ECO:0000255|HAMAP-Rule:MF_00535}; OrderedLocusNames=H16_B0046;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC ammonia and carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_00535}.
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_00535};
CC -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000255|HAMAP-
CC Rule:MF_00535}.
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; AM260480; CAJ94852.1; -; Genomic_DNA.
DR RefSeq; WP_010811104.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0K572; -.
DR SMR; Q0K572; -.
DR STRING; 381666.H16_B0046; -.
DR EnsemblBacteria; CAJ94852; CAJ94852; H16_B0046.
DR GeneID; 57645924; -.
DR KEGG; reh:H16_B0046; -.
DR eggNOG; COG1513; Bacteria.
DR HOGENOM; CLU_103452_1_0_4; -.
DR OMA; FLPYKAW; -.
DR OrthoDB; 1506439at2; -.
DR Proteomes; UP000008210; Chromosome 2.
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..147
FT /note="Cyanate hydratase"
FT /id="PRO_1000072537"
FT ACT_SITE 88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT ACT_SITE 91
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
SQ SEQUENCE 147 AA; 16578 MW; 8F431573D3B46674 CRC64;
MNRSDVTDLI IEAKVTRGIA WAQVAERVGR SKEWTTAACL GQMAFDAAGA RAVMELFGLP
PEAEPWLREV PYKGSLPTQV PADPLIYRFY ELISVYGTTF KALIHEEFGD GIMSAIDFRM
DLQREPDPNG DRVRIEMSGK FLPYKTY
