Reviewed, UniProtKB/Swiss-Prot A7ZCQ2 (ISPDF_CAMC1)

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:	Ccon26_06810
ORF Names:	CCC13826_1467

Organism

Campylobacter concisus (strain 13826) [Complete proteome] [HAMAP]

Taxonomic identifier

360104 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	372 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 – 372	372	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_1000073539
Regions
	Region	1 – 211	211	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	212 – 372	161	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	218	1	Divalent metal cation By similarity
	Metal binding	220	1	Divalent metal cation By similarity
	Metal binding	252	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	244	1	Transition state stabilizer By similarity
	Site	343	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZCQ2-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: B9AA9BD212BB03C7	FASTA	372	40,938
	10 20 30 40 50 60 MLDISLIMLG AGNSSRFELP VKKQWLRIGS DPLWLFATKN LSNFYTFKEI IVVSKECKYM 70 80 90 100 110 120 SKFAPNYKFV DGGETRQDSL KNALELVSSE FVLVSDIARP CISSELFHKI IEAAAQADCV 130 140 150 160 170 180 VPALKIADTA YLGENAIDRE KVKLIQTPQL SRTTLLKKAL SSGEIYTDDS SAMRAIGASV 190 200 210 220 230 240 WHILGDEMAR KITFKEDLVK ISALKAPENE LFVGSGFDVH EFEKGRPLVL CGEKIDYEFG 250 260 270 280 290 300 LKAHSDGDVA LHALTDAILG AAGLGDIGEL FPDTDDKFKD ISSIYLLQEA YKRVQSVGFV 310 320 330 340 350 360 LTNADITIMA QKPKLSKLKS KMEANIAQAL NLSQSRINVK ATTTEGLGFV GRCEGIAVMA 370 SASLKFYNWT QI

References

[1]	"Genome sequence of Campylobacter concisus 13826 isolated from human feces." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000792 Genomic DNA. Translation: EAT97612.1.
RefSeq	YP_001466560.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZCQ2.
Genome annotation databases
GeneID	5597562.
GenomeReviews	Gene locus Ccon26_06810 in contig CP000792_GR.
KEGG	cco:CCC13826_1467.
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. False negative. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_CAMC1

Accession

Primary (citable) accession number: A7ZCQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	October 23, 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)