Reviewed, UniProtKB/Swiss-Prot Q17WU1 (ISPDF_HELAH)

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:	Hac_1124

Organism

Helicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]

Taxonomic identifier

382638 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
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. HAMAP MF_01520
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. HAMAP MF_01520
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_0000296746
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)
	Q17WU1-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 865F215DFFDE49DF	FASTA	406	45,513
	10 20 30 40 50 60 MSLIRVNGEA FNLSLESLKE DPFETKKTLE TLIKQTSVIL LAAGESRRFS QTIKKQWLRS 70 80 90 100 110 120 NHTPLWLSVY ESFTEALDFK EVILVVSELD YTYIKRHYPK IKLVRGGISR QESVCNALKV 130 140 150 160 170 180 ISGAYTLTSD VARGLANIEM LNDLFLTLQN TNHYCIAPYL PCYDTAIYYN EALDREAIKL 190 200 210 220 230 240 IQTPQLSHTK TLQLALNQGD FKDESSAILQ AFPDLVSYIE GSKDLHKLTT SDDLKIFTPF 250 260 270 280 290 300 FNPAKDTFIG MGFDTHAFIK DKPMVLGGVV LDCEFGLKAH SDGDALLHAM IDAILGAIKG 310 320 330 340 350 360 GDIGEWFPDN DPKYKNASSK ELLKIVLDFS QSIGFELFEM GATIFSEIPK ITPYKPAILE 370 380 390 400 NLSQLLGLEK SQISLKATTM EKMGFIGQQE GLLVQAHASM RYKQKL

References

[1]

"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines." Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C. PLoS Genet. 2:1097-1110(2006) [PubMed: 16789826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM260522 Genomic DNA. Translation: CAJ99885.1.
RefSeq	YP_664884.1.
3D structure databases
SMR	Q17WU1. Positions 35-404.
ModBase	Search...
Protein-protein interaction databases
STRING	Q17WU1.
Genome annotation databases
GeneID	4176130.
GenomeReviews	Gene locus Hac_1124 in contig AM260522_GR.
KEGG	hac:Hac_1124.
NMPDR	fig|382638.8.peg.1092.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1211.
HOGENOM	HBG672839.
OMA	GGDIGEW.
PhylomeDB	Q17WU1.
Enzyme and pathway databases
BioCyc	HACI382638:HAC_1124-MONOMER.
Family and domain databases
HAMAP	MF_01520. IspDF. [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_HELAH

Accession

Primary (citable) accession number: Q17WU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 25, 2006
Last modified:	February 9, 2010
This is version 27 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)