P83700 (ISPE_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Short name=CMK
EC=2.7.1.148

Alternative name(s):
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase

Gene names

Name:	ispE
Ordered Locus Names:	TTHA0170

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. HAMAP MF_00061
Catalytic activity	ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Ref.2
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. HAMAP MF_00061
Sequence similarities	Belongs to the GHMP kinase family. IspE subfamily.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	terpenoid biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 275

275

4-diphosphocytidyl-2-C-methyl-D-erythritol kinase HAMAP MF_00061

PRO_0000189279

Regions

Nucleotide binding

86 – 96

11

ATP Potential

Sites

Active site

8

1

Probable

Active site

125

1

Probable

Secondary structure

1

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275

Helix Strand Turn

Details...

Beta strand

2 – 18

17

Beta strand

22 – 46

25

Beta strand

48 – 52

5

Helix

55 – 57

3

Helix

59 – 70

12

Beta strand

76 – 82

7

Beta strand

87 – 91

5

Helix

93 – 108

16

Helix

115 – 122

8

Helix

126 – 131

6

Beta strand

133 – 138

6

Turn

139 – 142

4

Beta strand

143 – 147

5

Beta strand

152 – 158

7

Helix

165 – 170

6

Helix

174 – 176

3

Helix

183 – 192

10

Helix

203 – 209

7

Helix

212 – 222

11

Beta strand

226 – 230

5

Beta strand

237 – 240

4

Helix

244 – 254

11

Turn

255 – 257

3

Beta strand

258 – 265

8

Sequences

	Sequence		Length	Mass (Da)
	P83700 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: FBD398F091167202	FASTA	275	29,253
	10 20 30 40 50 60 MERLAPAKVN LGLSVRFRRE DGYHELHTLF APFSLADRLV VEPVSSGLHF QGPYGRENLA 70 80 90 100 110 120 YRAASLYLEA AGQPGGVRIL LEKRIPEGAG LGGGSSDAAQ VLLALQALYP AEVDLFALAR 130 140 150 160 170 180 TLGADVPFFL LGRGAEARGV GERLKPLALP PVPAVVFFPG LRVPTPLVYR AVRPEDFGPD 190 200 210 220 230 240 LPVEAILEAL ARGEEPPYWN SLEGPAFRLF PELKEVRGRM RALGLRGVLM SGSGSAFFGL 250 260 270 AEGPDHARRA AEALRAWGRA WAGTLGGGDA GSGPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis." Wada T., Kuzuyama T., Satoh S., Kuramitsu S., Yokoyama S., Unzai S., Tame J.R.H., Park S.-Y. J. Biol. Chem. 278:30022-30027(2003) [PubMed: 12771135] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD69993.1.

RefSeq

YP_143436.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UEK	X-ray	1.70	A	1-275	[»]

ProteinModelPortal

P83700.

SMR

P83700. Positions 1-268.

ModBase

Search...

Protein-protein interaction databases

STRING

P83700.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3169608.

GenomeReviews

Gene locus TTHA0170 in contig AP008226_GR.

KEGG

ttj:TTHA0170.

PATRIC

23955281. VBITheThe93045_0168.

Phylogenomic databases

eggNOG

COG1947.

HOGENOM

HBG734593.

OMA

VSTAEVY.

PhylomeDB

P83700.

ProtClustDB

PRK14612.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0170-MONOMER.

Family and domain databases

HAMAP

MF_00061. IspE.
[Tree]

InterPro

IPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR004424. IspE.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

Gene3D

G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

KO

K00919.

PANTHER

PTHR20861:SF2. IspE. 1 hit.

Pfam

PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]

PIRSF

PIRSF010376. IspE. 1 hit.

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00154. IspE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ISPE_THET8

Accession

Primary (citable) accession number: P83700
Secondary accession number(s): Q5SLX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program