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Database: UniProt
Entry: A0A498R9F9_9FIRM
LinkDB: A0A498R9F9_9FIRM
Original site: A0A498R9F9_9FIRM 
ID   A0A498R9F9_9FIRM        Unreviewed;       161 AA.
AC   A0A498R9F9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Cyanate hydratase {ECO:0000256|HAMAP-Rule:MF_00535};
DE            Short=Cyanase {ECO:0000256|HAMAP-Rule:MF_00535};
DE            EC=4.2.1.104 {ECO:0000256|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate hydrolase {ECO:0000256|HAMAP-Rule:MF_00535};
DE   AltName: Full=Cyanate lyase {ECO:0000256|HAMAP-Rule:MF_00535};
GN   Name=cynS {ECO:0000256|HAMAP-Rule:MF_00535};
GN   ORFNames=LUCI_2852 {ECO:0000313|EMBL:VBB07587.1};
OS   Lucifera butyrica.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Lucifera.
OX   NCBI_TaxID=1351585 {ECO:0000313|EMBL:VBB07587.1, ECO:0000313|Proteomes:UP000277811};
RN   [1] {ECO:0000313|EMBL:VBB07587.1, ECO:0000313|Proteomes:UP000277811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUCI {ECO:0000313|EMBL:VBB07587.1};
RA   Strepis N.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC       ammonia and carbon dioxide. {ECO:0000256|ARBA:ARBA00003561,
CC       ECO:0000256|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:0000256|HAMAP-Rule:MF_00535};
CC   -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00535}.
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DR   EMBL; UPPP01000076; VBB07587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498R9F9; -.
DR   OrthoDB; 9785870at2; -.
DR   Proteomes; UP000277811; 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; 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; IPR048564; CYNS_N.
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   Pfam; PF21291; CYNS_N; 1.
DR   PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR   PRINTS; PR01693; CYANASE.
DR   SMART; SM01116; Cyanate_lyase; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF55234; Cyanase C-terminal domain; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00535};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277811}.
FT   DOMAIN          23..77
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00535"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00535"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00535"
SQ   SEQUENCE   161 AA;  18275 MW;  50B8C055C384DEB0 CRC64;
     MSATPVNNRD YLWDYREKAL AVLEKARLEK GLSYEEIAKK LEVSKVWLAS TFKGQQFVPA
     DYTEKLATIL GLSIADVRVL QEHPYKGNVD PILYRLHEVF DTYGPAIKAI IHEKFGDGNG
     IMSAIDFSVD VEKVEDPKGD RVVITFNGKF LPYSCKGKYP W
//
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