KCY2_BORGP
ID KCY2_BORGP Reviewed; 178 AA.
AC Q65ZV5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytidylate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00239};
DE Short=CK 2 {ECO:0000255|HAMAP-Rule:MF_00239};
DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00239};
DE AltName: Full=Cytidine monophosphate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00239};
DE Short=CMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_00239};
GN Name=cmk2 {ECO:0000255|HAMAP-Rule:MF_00239}; OrderedLocusNames=BG0844;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00239};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00239};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00239}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00239}.
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DR EMBL; CP000013; AAU07666.1; -; Genomic_DNA.
DR RefSeq; WP_011194110.1; NZ_CP028872.1.
DR AlphaFoldDB; Q65ZV5; -.
DR SMR; Q65ZV5; -.
DR STRING; 290434.BG0844; -.
DR EnsemblBacteria; AAU07666; AAU07666; BG0844.
DR KEGG; bga:BG0844; -.
DR eggNOG; COG1102; Bacteria.
DR HOGENOM; CLU_079959_1_0_12; -.
DR OMA; FIFRDMA; -.
DR OrthoDB; 1392851at2; -.
DR Proteomes; UP000002276; 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..178
FT /note="Cytidylate kinase 2"
FT /id="PRO_0000132029"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ SEQUENCE 178 AA; 20850 MW; 467DDD9D6A1273E7 CRC64;
MKIALSGKSG CGNTTVSSMI AKHYGLEFIN YTFHDIARER NIPFSEFYEK EIIGRDDYYW
DMYLDKRLSL LSKKNNTVLA SRLAIWISKS ADLKIYLYAK MEVRAERIMT REGGMYSDVL
SSTFNRDEND KKRYLSIYNI DIDDYSSKTD LVIDVTNINS NEVFELIRDE IDKRNLKN