Reviewed, UniProtKB/Swiss-Prot Q8FI04 (ISPE_ECOL6)

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:	c1666

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Catalytic activity	ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_00061
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. HAMAP MF_00061
Subunit structure	Homodimer. Ref.2
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
Gene Ontology (GO)
Biological process	phosphorylation Inferred from electronic annotation. Source: InterPro terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity Inferred from electronic annotation. Source: HAMAP ATP binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

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

PRO_0000189217

Regions

Nucleotide binding

99 – 109

11

ATP Potential

Sites

Active site

10

1

Probable

Active site

141

1

Probable

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

2 – 20

19

Beta strand

26 – 49

24

Beta strand

51 – 53

3

Helix

62 – 64

3

Helix

66 – 80

15

Beta strand

89 – 95

7

Helix

106 – 121

16

Helix

128 – 135

8

Helix

136 – 138

3

Helix

142 – 147

6

Beta strand

151 – 154

4

Turn

155 – 158

4

Beta strand

159 – 162

4

Beta strand

169 – 173

5

Helix

181 – 185

5

Helix

199 – 204

6

Helix

212 – 218

7

Helix

220 – 229

10

Turn

230 – 232

3

Beta strand

235 – 237

3

Beta strand

244 – 250

7

Helix

251 – 260

10

Helix

263 – 265

3

Beta strand

268 – 275

8

Helix

277 – 280

4

Sequences

	Sequence		Length	Mass (Da)
	Q8FI04-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: E0327295E65EDDFC	FASTA	283	30,973
	10 20 30 40 50 60 MRTQWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT ISIELRDDGD IRLLTPVEGV 70 80 90 100 110 120 EHEDNLIVRA ARLLMKTAAD SGRLSTGSGA NISIDKRLPM GGGLGGGSSN AATVLVALNH 130 140 150 160 170 180 LWQCGLSMDE LAEMGLTLGA DVPVFVRGHA AFAEGVGEIL MPVDPPEKWY LVAHPGVSIP 190 200 210 220 230 240 TPVIFKDPEL PRNTPKRSIE TLLKCEFSND CEVIARKRFR EVDAVLSWLL EYAPSRLTGT 250 260 270 280 GACVFAEFDT ESEARQVLEQ APEWLNGFVA KGVNLSPLHR AML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.
[2]	"Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase." Miallau L., Alphey M.S., Kemp L.E., Leonard G.A., McSweeney S.M., Hecht S., Bacher A., Eisenreich W., Rohdich F., Hunter W.N. Proc. Natl. Acad. Sci. U.S.A. 100:9173-9178(2003) [PubMed: 12878729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE014075 Genomic DNA. Translation: AAN80131.1.

RefSeq

NP_753571.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OJ4	X-ray	2.01	A/B	1-283	[»]

ModBase

Search...

Genome annotation databases

GeneID

1035444.

GenomeReviews

Gene locus c1666 in contig AE014075_GR.

KEGG

ecc:c1666.

NMPDR

fig|199310.1.peg.1614.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q8FI04.

OMA

PMGGGIG.

Enzyme and pathway databases

BRENDA

2.7.1.148. 292881.

Family and domain databases

HAMAP

MF_00061.
[Tree]

InterPro

IPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR004424. IspE.
[Graphical view]

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.

TIGRFAMs

TIGR00154. ispE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ISPE_ECOL6

Accession

Primary (citable) accession number: Q8FI04

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)