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Database: UniProt
Entry: KCY_THET8
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ID   KCY_THET8               Reviewed;         208 AA.
AC   Q5SL35;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=TTHA0458;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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; 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}.
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DR   EMBL; AP008226; BAD70281.1; -; Genomic_DNA.
DR   RefSeq; WP_011227951.1; NC_006461.1.
DR   RefSeq; YP_143724.1; NC_006461.1.
DR   PDB; 3AKC; X-ray; 1.65 A; A=1-208.
DR   PDB; 3AKD; X-ray; 1.60 A; A=1-208.
DR   PDB; 3W8N; X-ray; 2.20 A; A=1-208.
DR   PDB; 3W90; X-ray; 1.65 A; A=1-208.
DR   PDB; 7CKJ; X-ray; 1.50 A; A=1-208.
DR   PDBsum; 3AKC; -.
DR   PDBsum; 3AKD; -.
DR   PDBsum; 3W8N; -.
DR   PDBsum; 3W90; -.
DR   PDBsum; 7CKJ; -.
DR   AlphaFoldDB; Q5SL35; -.
DR   SMR; Q5SL35; -.
DR   EnsemblBacteria; BAD70281; BAD70281; BAD70281.
DR   GeneID; 3170130; -.
DR   KEGG; ttj:TTHA0458; -.
DR   PATRIC; fig|300852.9.peg.457; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_0_0; -.
DR   PhylomeDB; Q5SL35; -.
DR   Proteomes; UP000000532; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000048310"
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           33..47
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           54..63
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           91..101
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           104..116
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           146..155
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           161..173
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:3AKC"
FT   STRAND          186..189
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:7CKJ"
FT   HELIX           195..207
FT                   /evidence="ECO:0007829|PDB:7CKJ"
SQ   SEQUENCE   208 AA;  22554 MW;  9D3B0F6BB95E0B84 CRC64;
     MRGIVTIDGP SASGKSSVAR RVAAALGVPY LSSGLLYRAA AFLALRAGVD PGDEEGLLAL
     LEGLGVRLLA QAEGNRVLAD GEDLTSFLHT PEVDRVVSAV ARLPGVRAWV NRRLKEVPPP
     FVAEGRDMGT AVFPEAAHKF YLTASPEVRA WRRARERPQA YEEVLRDLLR RDERDKAQSA
     PAPDALVLDT GGMTLDEVVA WVLAHIRR
//
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