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KCY_PYRHO
ID   KCY_PYRHO               Reviewed;         192 AA.
AC   O58988;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Cytidylate kinase;
DE            Short=CK;
DE            EC=2.7.4.25;
DE   AltName: Full=Cytidine monophosphate kinase;
DE            Short=CMP kinase;
GN   Name=cmk; OrderedLocusNames=PH1265; ORFNames=PHBJ009;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000001; BAA30368.1; -; Genomic_DNA.
DR   PIR; F71071; F71071.
DR   RefSeq; WP_010885356.1; NC_000961.1.
DR   AlphaFoldDB; O58988; -.
DR   SMR; O58988; -.
DR   STRING; 70601.3257685; -.
DR   EnsemblBacteria; BAA30368; BAA30368; BAA30368.
DR   GeneID; 1443591; -.
DR   KEGG; pho:PH1265; -.
DR   eggNOG; arCOG01037; Archaea.
DR   OMA; FIFRDMA; -.
DR   OrthoDB; 110333at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02173; cyt_kin_arch; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..192
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_0000132021"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21625 MW;  6565D429DE28DF54 CRC64;
     MPKDKLVITV SGLAGSGTTT LSKKIAEHYG LKHVYAGLIF RQMAKEKGMS LEEFQKYAEL
     HPEIDREVDR RQIEAAKEGN VVIEGRLAGW MVKNADLKIW LDAPIRVRAE RVAKREGISV
     EEAFMKIAER EMQNRKRYLN LYGIDINDLS IYDLIINTSK WSPEGVFAIV KAAIDHLDPV
     GDAGSKKEKE VG
 
 
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