Reviewed, UniProtKB/Swiss-Prot O67060 (ISPE_AQUAE)

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:	aq_915

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	268 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
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 – 268

268

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

PRO_0000189183

Regions

Nucleotide binding

88 – 98

11

ATP Potential

Sites

Active site

9

1

By similarity

Active site

130

1

By similarity

Secondary structure

1

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268

Helix Strand Turn

Details...

Beta strand

2 – 19

18

Beta strand

25 – 46

22

Beta strand

48 – 51

4

Helix

57 – 59

3

Helix

61 – 73

13

Beta strand

79 – 84

6

Beta strand

91 – 93

3

Helix

95 – 110

16

Helix

117 – 127

11

Turn

129 – 131

3

Helix

132 – 135

4

Beta strand

138 – 143

6

Turn

144 – 147

4

Beta strand

148 – 151

4

Beta strand

158 – 164

7

Helix

171 – 175

5

Helix

180 – 182

3

Helix

186 – 197

12

Helix

201 – 203

3

Helix

207 – 215

9

Helix

217 – 228

12

Beta strand

242 – 246

5

Helix

250 – 259

10

Sequences

	Sequence		Length	Mass (Da)
	O67060-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: C905F9B988E0B45D	FASTA	268	29,788
	10 20 30 40 50 60 MIKVLSPAKI NLGLWVLGRL PSGYHEILTL YQEIPFYDEI YIREGVLRVE TNIGIPQEEN 70 80 90 100 110 120 LVYKGLREFE RITGIEINYS IFIQKNIPPG AGLGGGSSNL AVVLKKVNEL LGSPLSEEEL 130 140 150 160 170 180 RELVGSISAD APFFLLGKSA IGRGKGEVLE PVETEISGKI TLVIPQVSSS TGRVYSSLRE 190 200 210 220 230 240 EHFVTPEYAE EKIQRIISGE VEEIENVLGD IARELYPEIN EVYRFVEYLG FKPFVSGSGS 250 260 TVYFFGGASE ELKKAAKMRG WKVVELEL

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000657 Genomic DNA. Translation: AAC07027.1.

PIR

A70379.

RefSeq

NP_213622.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V2Q	X-ray	2.30	A/B	1-268	[»]
2V2V	X-ray	2.40	A/B	1-268	[»]
2V2Z	X-ray	2.25	A/B	1-268	[»]
2V34	X-ray	2.30	A/B	1-268	[»]
2V8P	X-ray	2.10	A/B	1-268	[»]
2VF3	X-ray	2.20	A/B	1-268	[»]

ModBase

Search...

Genome annotation databases

GeneID

1193602.

GenomeReviews

Gene locus aq_915 in contig AE000657_GR.

KEGG

aae:aq_915.

NMPDR

fig|224324.1.peg.637.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

O67060.

OMA

NDPITIA.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_915-MON.

BRENDA

2.7.1.148. 189781.

Family and domain databases

HAMAP

MF_00061.
[Tree]

InterPro

IPR006204. GHMP_kinase.
IPR004424. IspE.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

Gene3D

G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

PANTHER

PTHR20861:SF2. IspE. 1 hit.

Pfam

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_AQUAE

Accession

Primary (citable) accession number: O67060

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	November 3, 2009
This is version 59 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)