2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
     (EC 2.7.7.60)
     (4-diphosphocytidyl-2C-methyl-D-erythritol synthase)
     (MEP cytidylyltransferase)
     (MCT)
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
     (MECPS)
     (MECDP-synthase)
     (EC 4.6.1.12)

Gene name

	Name:	ispDF
	OrderedLocusNames:	RHE_CH01945

From

Rhizobium etli (strain CFN 42 / ATCC 51251)

[TaxID: 347834]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0508502103; PubMed=16505379 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.;
"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons.";
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).

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.
CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP.
COFACTOR: Divalent metal cations (By similarity).
PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 2/6 .
PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 4/6 .
SIMILARITY: In the N-terminal section; belongs to the ispD family.
SIMILARITY: In the C-terminal section; belongs to the ispF family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000133; ABC90731.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_469458.1; -.

3D structure databases

ModBase

Q2K8V5.

Ontologies

GO:0008685;	Molecular function: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity (inferred from electronic annotation from HAMAP).
GO:0050518;	Molecular function: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016114;	Biological process: terpenoid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01520; -; 1.
PBIL [Tree]

InterPro

IPR001228; ISPD_synthase.
IPR003526; MECDP_synthase_core.
Graphical view of domain structure.

Pfam

PF01128; IspD; 1.
PF02542; YgbB; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00453; ispD; 1.
TIGR00151; ispF; 1.

PROSITE

PS01295; ISPD; 1.
PS01350; ISPF; 1.

ProtoNet

Q2K8V5.

Genome annotation databases

GeneID

3893983; -.

GenomeReviews

CP000133_GR; RHE_CH01945.

KEGG

ret:RHE_CH01945; -.

Phylogenomic databases

HOGENOM

Q2K8V5; -.

Genome annotation databases

CMR

Q2K8V5; RHE_CH01945.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 406`	`406`	`Bifunctional enzyme ispD/ispF.`	`PRO_0000292859`
`REGION`	`1 246`	`246`	`2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.`
`REGION`	`247 406`	`160`	`2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.`
`METAL`	`253 253`		`Divalent metal cation (By similarity).`
`METAL`	`255 255`		`Divalent metal cation (By similarity).`
`METAL`	`287 287`		`Divalent metal cation (By similarity).`
`SITE`	`24 24`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`33 33`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`167 167`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`224 224`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`279 279`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`378 378`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 43763 Da [This is the MW of the unprocessed precursor]

CRC64: 44A00BC422A9197E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLQMPSKQPI SAGIVVVAAG RGERAGSSTE GPKQYRMIGG KPVIVHTLEN FMTWEAAKQI 

        70         80         90        100        110        120 
VVVIHPDDEA LFAKASRHII SETPIETVHG GATRQESVLA GLRYLKDKHV SHVLIHDAVR 

       130        140        150        160        170        180 
PFFDHVLLDR IAERLGNGAP AVLPAMPVTD TLKRADSAGT ISATVSREHL YAAQTPQSFV 

       190        200        210        220        230        240 
FETILDAHEK AAASGRSDFT DDASIAEWSG IPVTVVEGTP DNVKLTLRSD IAMADDKLSA 

       250        260        270        280        290        300 
PMLPDVRTGN GYDVHQLEPG DGVTLCGVFI PHDQRLKGHS DADVALHALT DALLATCGAG 

       310        320        330        340        350        360 
DIGDHFPPSD PQWKGAASKI FIEHAARIVR ERGGTIMNAD VSLIAEAPKV GPHREAMRAR 

       370        380        390        400 
LSEYLGIDIE RCSVKATTNE KIGFVGRREG IAAIATATVV YRWRKR

Q2K8V5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools