KCY_MYCTU
ID KCY_MYCTU Reviewed; 230 AA.
AC P9WPA9; L0TAE5; O33211; P63803;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238};
GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=Rv1712;
GN ORFNames=MTCI125.34;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-17, CATALYTIC ACTIVITY, SUBUNIT, MASS SPECTROMETRY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RX PubMed=19181797; DOI=10.1128/jb.01337-08;
RA Thum C., Schneider C.Z., Palma M.S., Santos D.S., Basso L.A.;
RT "The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a
RT functional CMP kinase that preferentially phosphorylates dCMP.";
RL J. Bacteriol. 191:2884-2887(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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_00238, ECO:0000269|PubMed:19181797};
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_00238, ECO:0000269|PubMed:19181797};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for CMP {ECO:0000269|PubMed:19181797};
CC KM=165 uM for dCMP {ECO:0000269|PubMed:19181797};
CC KM=13.9 mM for UMP {ECO:0000269|PubMed:19181797};
CC Vmax=131 umol/min/mg enzyme with CMP as substrate
CC {ECO:0000269|PubMed:19181797};
CC Vmax=75 umol/min/mg enzyme with dCMP as substrate
CC {ECO:0000269|PubMed:19181797};
CC Vmax=32 umol/min/mg enzyme with UMP as substrate
CC {ECO:0000269|PubMed:19181797};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19181797}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC -!- MASS SPECTROMETRY: Mass=23930.56; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19181797};
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00238}.
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DR EMBL; AL123456; CCP44478.1; -; Genomic_DNA.
DR PIR; G70504; G70504.
DR RefSeq; NP_216228.1; NC_000962.3.
DR RefSeq; WP_003408441.1; NZ_NVQJ01000010.1.
DR AlphaFoldDB; P9WPA9; -.
DR SMR; P9WPA9; -.
DR STRING; 83332.Rv1712; -.
DR PaxDb; P9WPA9; -.
DR DNASU; 885157; -.
DR GeneID; 45425683; -.
DR GeneID; 885157; -.
DR KEGG; mtu:Rv1712; -.
DR TubercuList; Rv1712; -.
DR eggNOG; COG0283; Bacteria.
DR OMA; RAITWWM; -.
DR PhylomeDB; P9WPA9; -.
DR BRENDA; 2.7.4.25; 3445.
DR SABIO-RK; P9WPA9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; IDA:MTBBASE.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central.
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_00238; Cytidyl_kinase_type1; 1.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00017; cmk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19181797"
FT CHAIN 2..230
FT /note="Cytidylate kinase"
FT /id="PRO_0000131943"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ SEQUENCE 230 AA; 24177 MW; D1E6BF0354D13AA3 CRC64;
MSRLSAAVVA IDGPAGTGKS SVSRRLAREL GARFLDTGAM YRIVTLAVLR AGADPSDIAA
VETIASTVQM SLGYDPDGDS CYLAGEDVSV EIRGDAVTRA VSAVSSVPAV RTRLVELQRT
MAEGPGSIVV EGRDIGTVVF PDAPVKIFLT ASAETRARRR NAQNVAAGLA DDYDGVLADV
RRRDHLDSTR AVSPLQAAGD AVIVDTSDMT EAEVVAHLLE LVTRRSEAVR
