Reviewed, UniProtKB/Swiss-Prot B6JL03 (ISPDF_HELP2)

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:	HPP12_0424

Organism

Helicobacter pylori (strain P12) [Complete proteome] [HAMAP]

Taxonomic identifier

570508 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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) By similarity.
Catalytic activity	CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_01520 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520
Cofactor	Divalent metal cations By similarity.
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	Complete proteome 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_1000146272
Regions
	Region	1 – 247	247	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	248 – 406	159	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	254	1	Divalent metal cation By similarity
	Metal binding	256	1	Divalent metal cation By similarity
	Metal binding	288	1	Divalent metal cation By similarity
	Site	48	1	Transition state stabilizer By similarity
	Site	55	1	Transition state stabilizer By similarity
	Site	175	1	Positions MEP for the nucleophilic attack By similarity
	Site	227	1	Positions MEP for the nucleophilic attack By similarity
	Site	280	1	Transition state stabilizer By similarity
	Site	379	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6JL03-1 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 5D20A74AAB2E10FA	FASTA	406	45,531
	10 20 30 40 50 60 MSLIRVNGEA FKLSLESLEE DPFETKETLE TLVKQTSVVL LAAGESRRFS QIIKKQWLRS 70 80 90 100 110 120 NHTPLWLSVY ESFKEALDFK EILLIVSELD YIYIQRHYPE IKLVKGGASR QESVRNALKI 130 140 150 160 170 180 IDSTYTLTSD VARGLANMEA LKSLFLTLQQ TSHYCIAPYL PCYDTAIYYN EALDREAIKL 190 200 210 220 230 240 IQTPQLSHTK ALQSALNQGD FKDESSAILQ AFPNRVSYIE GSKNLHKLTT SGDLKHFALF 250 260 270 280 290 300 FNPAKDTFIG MGFDTHAFIK DKPMVLGGVV LDCEFGLKAH SDGDALLHAV IDAILGAIKG 310 320 330 340 350 360 GDIGEWFPDN DPKYKNASSK ELLKIVLDFS QSIGFELFEM GATIFSEIPK ITPYKPAILE 370 380 390 400 NLSQLLGLEK SQISLKATTM EKMGFIGKQE GLLVQAHVSM RYKQKL

References

[1]	"The complete genome sequence of Helicobacter pylori strain P12." Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001217 Genomic DNA. Translation: ACJ07581.1.
RefSeq	YP_002301061.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7010798.
GenomeReviews	Gene locus HPP12_0424 in contig CP001217_GR.
KEGG	hpp:HPP12_0424.
Organism-specific databases
CMR	Search...
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_HELP2

Accession

Primary (citable) accession number: B6JL03

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	December 16, 2008
Last modified:	October 13, 2009
This is version 10 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)