CYNS_SERP5
ID CYNS_SERP5 Reviewed; 156 AA.
AC A8GBZ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Spro_1533;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000826; ABV40637.1; -; Genomic_DNA.
DR RefSeq; WP_012005966.1; NC_009832.1.
DR PDB; 4Y42; X-ray; 2.09 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 6B6M; X-ray; 1.91 A; A/B/C/D/E=1-156.
DR PDBsum; 4Y42; -.
DR PDBsum; 6B6M; -.
DR AlphaFoldDB; A8GBZ7; -.
DR SMR; A8GBZ7; -.
DR STRING; 399741.Spro_1533; -.
DR EnsemblBacteria; ABV40637; ABV40637; Spro_1533.
DR KEGG; spe:Spro_1533; -.
DR eggNOG; COG1513; Bacteria.
DR HOGENOM; CLU_103452_1_1_6; -.
DR OMA; YELVMIN; -.
DR OrthoDB; 1506439at2; -.
DR BRENDA; 4.2.1.104; 8756.
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 1: Evidence at protein level;
KW 3D-structure; Lyase.
FT CHAIN 1..156
FT /note="Cyanate hydratase"
FT /id="PRO_1000061028"
FT ACT_SITE 96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT ACT_SITE 99
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00535"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6B6M"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:6B6M"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6B6M"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6B6M"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4Y42"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6B6M"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:6B6M"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:6B6M"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:6B6M"
FT STRAND 118..134
FT /evidence="ECO:0007829|PDB:6B6M"
FT STRAND 138..152
FT /evidence="ECO:0007829|PDB:6B6M"
SQ SEQUENCE 156 AA; 17154 MW; 64D7B5E882F5604D CRC64;
MTQSLHYSSP RETLTDTIMM AKIRKNLTFE AINQGTGLSL AFVTAALLGQ HPLPEQAARV
VAEKLDLDED AIRLLQTIPL RGSIPGGVPT DPTIYRFYEM VQIYGSTLKA LVHEQFGDGI
ISAINFKLDI KKVPDPDGGE RAVITLDGKY LPTKPF