Reviewed, UniProtKB/Swiss-Prot A8FNR8 (ISPDF_CAMJ8)

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:	C8J_1508

Organism

Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP]

Taxonomic identifier

407148 [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	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 – 371	371	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_1000073540
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

Sequences

	Sequence		Length	Mass (Da)
	A8FNR8-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 7E72D30FC89B2DBE	FASTA	371	41,658
	10 20 30 40 50 60 MSEISLIMLA 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 DKVREVGFEL 310 320 330 340 350 360 INIDICVMAQ SPKLKDFKQA MQSNIAHTLD LDEFRINVKA TTTEKLGFIG RKEGMAVLSS 370 VNLKYFDWTR L

References

[1]	"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)." Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M. J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000814 Genomic DNA. Translation: ABV53105.1.
RefSeq	YP_001483082.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8FNR8.
Genome annotation databases
GeneID	5618304.
GenomeReviews	Gene locus C8J_1508 in contig CP000814_GR.
KEGG	cju:C8J_1508.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IVLIHDA.
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_CAMJ8

Accession

Primary (citable) accession number: A8FNR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	November 13, 2007
Last modified:	November 3, 2009
This is version 15 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)