KCY_PYRAB
ID KCY_PYRAB Reviewed; 181 AA.
AC Q9UZJ6; G8ZKC4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, 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=PYRAB11500; ORFNames=PAB0763;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB50061.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70567.1; -; Genomic_DNA.
DR PIR; H75094; H75094.
DR RefSeq; WP_010868267.1; NC_000868.1.
DR AlphaFoldDB; Q9UZJ6; -.
DR SMR; Q9UZJ6; -.
DR STRING; 272844.PAB0763; -.
DR EnsemblBacteria; CAB50061; CAB50061; PAB0763.
DR GeneID; 1496513; -.
DR KEGG; pab:PAB0763; -.
DR PATRIC; fig|272844.11.peg.1208; -.
DR eggNOG; arCOG01037; Archaea.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; FIFRDMA; -.
DR OrthoDB; 110333at2157; -.
DR PhylomeDB; Q9UZJ6; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..181
FT /note="Cytidylate kinase"
FT /id="PRO_0000132018"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 20688 MW; DB2A0B3661027899 CRC64;
MPKGCLVITV SGLAGSGTTT LCRNLAKHYG FKHVYAGLIF RQMAKERGMS LEEFQKYAEL
HPEIDREVDR RQVEAAKECN VVIEGRLAGW MVKNADLKIW LDAPIRVRAE RVAKREGISV
EEAFMKIAER EMQNRKRYLN LYGIDINDLS IYDLIIDTSK WSPEGVFAIV KAAIDHLYEK
V
