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CYNS_POLAQ
ID   CYNS_POLAQ              Reviewed;         147 AA.
AC   A4SXJ6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Pnuc_0994;
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34210.1; -; Genomic_DNA.
DR   RefSeq; WP_011902835.1; NC_009379.1.
DR   AlphaFoldDB; A4SXJ6; -.
DR   SMR; A4SXJ6; -.
DR   STRING; 312153.Pnuc_0994; -.
DR   EnsemblBacteria; ABP34210; ABP34210; Pnuc_0994.
DR   GeneID; 31481366; -.
DR   KEGG; pnu:Pnuc_0994; -.
DR   eggNOG; COG1513; Bacteria.
DR   HOGENOM; CLU_103452_1_0_4; -.
DR   OMA; EWTTAAM; -.
DR   Proteomes; UP000000231; Chromosome.
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.
FT   CHAIN           1..147
FT                   /note="Cyanate hydratase"
FT                   /id="PRO_1000081864"
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;  16576 MW;  186A112E1F60B329 CRC64;
     MDRSVVTQKI IEAKVRNGMK WSDIAKAIGE SKEWVTAGCL GQMTFTKVQA EAAGKLFDLT
     DEEMAWLQIV PYKGSLPTAV PTDPLIYRWY EIVSVYGTTI KELIHEEFGD GIMSAIDFSM
     DIQREPDPKG DRVQVVLSGK YLSYKTY
 
 
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