ISPE_THET8
ID ISPE_THET8 Reviewed; 275 AA.
AC P83700; Q5SLX3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE Short=CMK;
DE EC=2.7.1.148;
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN Name=ispE; OrderedLocusNames=TTHA0170;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; 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.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=12771135; DOI=10.1074/jbc.m304339200;
RA Wada T., Kuzuyama T., Satoh S., Kuramitsu S., Yokoyama S., Unzai S.,
RA Tame J.R.H., Park S.-Y.;
RT "Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
RT kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.";
RL J. Biol. Chem. 278:30022-30027(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC {ECO:0000269|PubMed:12771135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC Evidence={ECO:0000269|PubMed:12771135};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6. {ECO:0000269|PubMed:12771135}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD69993.1; -; Genomic_DNA.
DR RefSeq; WP_011174171.1; NC_006461.1.
DR RefSeq; YP_143436.1; NC_006461.1.
DR PDB; 1UEK; X-ray; 1.70 A; A=1-275.
DR PDBsum; 1UEK; -.
DR AlphaFoldDB; P83700; -.
DR SMR; P83700; -.
DR STRING; 300852.55771552; -.
DR EnsemblBacteria; BAD69993; BAD69993; BAD69993.
DR GeneID; 3169608; -.
DR KEGG; ttj:TTHA0170; -.
DR PATRIC; fig|300852.9.peg.168; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_1_1_0; -.
DR OMA; RWPSPAK; -.
DR PhylomeDB; P83700; -.
DR UniPathway; UPA00056; UER00094.
DR EvolutionaryTrace; P83700; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00061; IspE; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF010376; IspE; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..275
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000189279"
FT ACT_SITE 8
FT /evidence="ECO:0000305"
FT ACT_SITE 125
FT /evidence="ECO:0000305"
FT BINDING 86..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..18
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 22..46
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1UEK"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1UEK"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1UEK"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1UEK"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1UEK"
SQ SEQUENCE 275 AA; 29253 MW; FBD398F091167202 CRC64;
MERLAPAKVN LGLSVRFRRE DGYHELHTLF APFSLADRLV VEPVSSGLHF QGPYGRENLA
YRAASLYLEA AGQPGGVRIL LEKRIPEGAG LGGGSSDAAQ VLLALQALYP AEVDLFALAR
TLGADVPFFL LGRGAEARGV GERLKPLALP PVPAVVFFPG LRVPTPLVYR AVRPEDFGPD
LPVEAILEAL ARGEEPPYWN SLEGPAFRLF PELKEVRGRM RALGLRGVLM SGSGSAFFGL
AEGPDHARRA AEALRAWGRA WAGTLGGGDA GSGPA
