ID A0A1G8A7J8_9BACL Unreviewed; 224 AA.
AC A0A1G8A7J8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN ORFNames=SAMN04487975_103128 {ECO:0000313|EMBL:SDH16924.1};
OS Planococcus glaciei.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=459472 {ECO:0000313|EMBL:SDH16924.1, ECO:0000313|Proteomes:UP000183022};
RN [1] {ECO:0000313|Proteomes:UP000183022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6846 {ECO:0000313|Proteomes:UP000183022};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP-
CC Rule:MF_00238};
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 Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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DR EMBL; FNDC01000003; SDH16924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8A7J8; -.
DR STRING; 459472.SAMN04487975_103128; -.
DR eggNOG; COG0283; Bacteria.
DR Proteomes; UP000183022; Unassembled WGS sequence.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00017; cmk; 1.
DR PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1.
DR PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00238}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:SDH16924.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00238}; Transferase {ECO:0000256|HAMAP-Rule:MF_00238}.
FT DOMAIN 7..219
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000259|Pfam:PF02224"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ SEQUENCE 224 AA; 24610 MW; 923BDE8AB1AD873A CRC64;
MTKSIQIALD GPAAAGKSTI AKIVAEQLGY IYIDTGAMYR AITLKALNEG IDLSDNKAAG
ELLAKTAIDL QPSENGQLVF LDQQNVTEAI RSQEVTGSVS EMAAHESVRL QMVKLQQQLA
EGRGVVMDGR DIGTDVLPKA ELKVFMSASV EERARRRFEE NKKRNIHTPL EELQGEIAKR
DQMDSEREVS PLRQADDAIY LDTTSLTIRE AAAEILRLAG ERLS
//
