Reviewed, UniProtKB/Swiss-Prot Q9PM68 (ISPDF_CAMJE)

Names and origin

Protein names

Recommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
              EC=2.7.7.60
        Alternative name(s):
            4-diphosphocytidyl-2C-methyl-D-erythritol synthase
            MEP cytidylyltransferase
              Short name=MCT
    2- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12

Gene names

Name:	ispDF
Ordered Locus Names:	Cj1607

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (ispD), and converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (ispF). HAMAP MF_01520
Catalytic activity	CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. Ref.2 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. Ref.2
Cofactor	Divalent metal cations. Ref.2
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Sequence similarities	In the N-terminal section; belongs to the ispD family. In the C-terminal section; belongs to the ispF family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding
Molecular function	Lyase Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: HAMAP 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliN	O32370	1	EBI-1192039,EBI-1191320

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 371

371

Bifunctional enzyme ispD/ispF HAMAP MF_01520

PRO_0000075662

Regions

Region

1 – 210

210

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520

Region

211 – 371

161

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding

217

1

Divalent metal cation By similarity

Metal binding

219

1

Divalent metal cation By similarity

Metal binding

251

1

Divalent metal cation By similarity

Site

16

1

Transition state stabilizer By similarity

Site

23

1

Transition state stabilizer By similarity

Site

139

1

Positions MEP for the nucleophilic attack By similarity

Site

191

1

Positions MEP for the nucleophilic attack By similarity

Site

243

1

Transition state stabilizer By similarity

Site

342

1

Transition state stabilizer By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

371

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Turn

15 – 17

3

Beta strand

19 – 21

3

Helix

23 – 25

3

Beta strand

27 – 29

3

Helix

33 – 42

10

Beta strand

50 – 55

6

Helix

57 – 61

5

Beta strand

65 – 71

7

Helix

76 – 84

9

Beta strand

89 – 96

8

Helix

104 – 111

8

Helix

112 – 116

5

Beta strand

118 – 124

7

Beta strand

130 – 132

3

Beta strand

135 – 137

3

Helix

139 – 141

3

Beta strand

142 – 145

4

Beta strand

149 – 152

4

Helix

153 – 159

7

Helix

169 – 174

6

Turn

175 – 177

3

Beta strand

180 – 184

5

Helix

187 – 189

3

Helix

195 – 200

6

Beta strand

210 – 225

16

Beta strand

227 – 229

3

Beta strand

232 – 240

9

Helix

248 – 260

13

Helix

266 – 269

4

Turn

276 – 279

4

Helix

282 – 295

14

Beta strand

298 – 308

11

Beta strand

310 – 312

3

Helix

315 – 317

3

Helix

318 – 329

12

Helix

333 – 335

3

Beta strand

336 – 341

6

Helix

347 – 350

4

Beta strand

353 – 365

13

Sequences

	Sequence		Length	Mass (Da)
	Q9PM68-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: BAD0087B19905FAF	FASTA	371	41,690
	10 20 30 40 50 60 MSEMSLIMLA AGNSTRFNTK VKKQFLRLGN DPLWLYATKN LSSFYPFKKI VVTSSNITYM 70 80 90 100 110 120 KKFTKNYEFI EGGDTRAESL KKALELIDSE FVMVSDVARV LVSKNLFDRL IENLDKADCI 130 140 150 160 170 180 TPALKVADTT LFDNEALQRE KIKLIQTPQI SKTKLLKKAL DQNLEFTDDS TAIAAMGGKI 190 200 210 220 230 240 WFVEGEENAR KLTFKEDLKK LDLPTPSFEI FTGNGFDVHE FGENRPLLLA GVQIHPTMGL 250 260 270 280 290 300 KAHSDGDVLA HSLTDAILGA AGLGDIGELY PDTDMKFKNA NSMELLKQAY DKVREIGFEL 310 320 330 340 350 360 INIDICVMAQ SPKLKDFKQA MQSNIAHTLD LDEFRINVKA TTTEKLGFIG RKEGMAVLSS 370 VNLKYFDWTR L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
[2]	"Biosynthesis of isoprenoids. A bifunctional IspDF enzyme from Campylobacter jejuni." Gabrielsen M., Rohdich F., Eisenreich W., Graewert T., Hecht S., Bacher A., Hunter W.N. Eur. J. Biochem. 271:3028-3035(2004) [PubMed: 15233799] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-22, CATALYTIC ACTIVITY, COFACTOR, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL111168 Genomic DNA. Translation: CAL35704.1.

PIR

E81256.

RefSeq

YP_002344976.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W55	X-ray	2.30	A	1-371	[»]
1W57	X-ray	3.09	A	1-371	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PM68. 29 interactions.

Genome annotation databases

GeneID

905874.

GenomeReviews

Gene locus Cj1607 in contig AL111168_GR.

KEGG

cje:Cj1607.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

IVLIHDA.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ1607-MON.

BRENDA

2.7.7.60. 255835.
4.6.1.12. 255835.

Family and domain databases

HAMAP

MF_01520.
[Tree]

InterPro

IPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]

Gene3D

G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.

Pfam

PF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.

PROSITE

PS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ISPDF_CAMJE

Accession

Primary (citable) accession number: Q9PM68
Secondary accession number(s): Q0P821

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 67 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)