KCY2_HAEIN
ID KCY2_HAEIN Reviewed; 222 AA.
AC P43893;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytidylate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CK 2 {ECO:0000255|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238};
GN Name=cmk2 {ECO:0000255|HAMAP-Rule:MF_00238}; Synonyms=cmkB;
GN OrderedLocusNames=HI_1646;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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};
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00238}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23293.1; ALT_INIT; Genomic_DNA.
DR PIR; H64134; H64134.
DR RefSeq; NP_439788.1; NC_000907.1.
DR AlphaFoldDB; P43893; -.
DR SMR; P43893; -.
DR STRING; 71421.HI_1646; -.
DR EnsemblBacteria; AAC23293; AAC23293; HI_1646.
DR KEGG; hin:HI_1646; -.
DR PATRIC; fig|71421.8.peg.1722; -.
DR eggNOG; COG0283; Bacteria.
DR HOGENOM; CLU_079959_2_0_6; -.
DR PhylomeDB; P43893; -.
DR BioCyc; HINF71421:G1GJ1-1663-MON; -.
DR Proteomes; UP000000579; 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; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..222
FT /note="Cytidylate kinase 2"
FT /id="PRO_0000131922"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ SEQUENCE 222 AA; 24368 MW; 1F9B12FE434D16F0 CRC64;
MIITVDGPSG AGKGTLCYAL AEKLGYALLD SGAIYRVTAL AALQRKTDLT NETDLAELAR
HLDIQFIPQN GEVNIFLAGM DVSRLIRTQE VADAASKVAV FQKVRSALLQ LQQDFAKNDG
LIADGRDMGT VVFPNAQVKL FLDASAEERA KRRYKQLQNK GINGNFAQIL AEIKERDFRD
RNREVAPLKP ADDAFYYSLN SSIISCAFFT ISSEPTNSGT RS