GenomeNet

Database: UniProt
Entry: KCY2_HAEIN
LinkDB: KCY2_HAEIN
Original site: 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   13-SEP-2023, entry version 120.
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; Pseudomonadota; 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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   OrthoDB; 9807434at2; -.
DR   PhylomeDB; P43893; -.
DR   BioCyc; HINF71421:G1GJ1-1663-MONOMER; -.
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; 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; 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
//
DBGET integrated database retrieval system