ID E7RQ26_9BACT Unreviewed; 245 AA.
AC E7RQ26;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ECO:0000313|EMBL:EFZ37219.1};
GN ORFNames=HMPREF0663_11277 {ECO:0000313|EMBL:EFZ37219.1};
OS Hoylesella oralis ATCC 33269.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ37219.1, ECO:0000313|Proteomes:UP000005580};
RN [1] {ECO:0000313|EMBL:EFZ37219.1, ECO:0000313|Proteomes:UP000005580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ37219.1,
RC ECO:0000313|Proteomes:UP000005580};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFZ37219.1}.
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DR EMBL; AEPE02000004; EFZ37219.1; -; Genomic_DNA.
DR AlphaFoldDB; E7RQ26; -.
DR STRING; 28134.SAMN05444288_1600; -.
DR eggNOG; COG0283; Bacteria.
DR HOGENOM; CLU_079959_0_2_10; -.
DR Proteomes; UP000005580; 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:EFZ37219.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00238}; Reference proteome {ECO:0000313|Proteomes:UP000005580};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:EFZ37219.1}.
FT DOMAIN 22..232
FT /note="Cytidylate kinase"
FT /evidence="ECO:0000259|Pfam:PF02224"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ SEQUENCE 245 AA; 28004 MW; E6070F9998460766 CRC64;
MLQQEQARNV SEYTENMKKI IIAIDGYSSC GKSTMAKDLA REIGYIYVDT GAMYRAVTLY
ALRKDLFRPD GSVKTGELEA CMPDIDISFR LNKETMRPDT YLNGELIEHE IRTLEVSSHV
SPIAAVPFVR HALVAQQQQM GKEKGIVMDG RDIGTTVFPH AELKIFVTAS AEVRAQRRFD
ELKAKGMPAR FNDILRNVQE RDYIDTHREI SPLRRAEDAI LLDNSNMTID QQRQWLIDRY
NECVG
//
