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:	Adeh_1272

From

Anaeromyxobacter dehalogenans (strain 2CP-C)

[TaxID: 290397]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Cystobacterineae; Myxococcaceae; Anaeromyxobacter.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.

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

CP000251; ABC81046.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_464483.1; -.

3D structure databases

ModBase

Q2IQG8.

Enzyme and pathway databases

BioCyc

ADEH290397:ADEH_1272-MON; -.

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; FALSE_NEG.

ProtoNet

Q2IQG8.

Genome annotation databases

GeneID

3888705; -.

GenomeReviews

CP000251_GR; Adeh_1272.

KEGG

ade:Adeh_1272; -.

Phylogenomic databases

HOGENOM

Q2IQG8; -.

Genome annotation databases

CMR

Q2IQG8; Adeh_1272.

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`	`1 386`	`386`	`Bifunctional enzyme ispD/ispF.`	`PRO_0000296738`
`REGION`	`1 229`	`229`	`2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.`
`REGION`	`230 386`	`157`	`2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.`
`METAL`	`236 236`		`Divalent metal cation (By similarity).`
`METAL`	`238 238`		`Divalent metal cation (By similarity).`
`METAL`	`269 269`		`Divalent metal cation (By similarity).`
`SITE`	`19 19`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`24 24`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`155 155`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`211 211`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`261 261`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`360 360`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 386 AA [This is the length of the unprocessed precursor]

Molecular weight: 39134 Da [This is the MW of the unprocessed precursor]

CRC64: 6FEF0790B3FD25E4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIRGERVIGI LAAGGSGQRA GVAKQWLVLG GESVLRRSAR VLAACDAVDG LVVVVPPGDE 

        70         80         90        100        110        120 
ARGEAELAGL GKPVRAVAGG PARADSVRNG LAAADGAVVL VHDAARPFAS AALAGRVAEA 

       130        140        150        160        170        180 
AARDGAALAA LPATDTVKRA EAGAEVPRVL ETLDRRTVWL AQTPQGFRRA VLEQAYAAAG 

       190        200        210        220        230        240 
PSASAATDEC ALVEAAGAPV TLVPGEPGNF KITGPDDVRR ARALLEAPVA TGVGYDTHRF 

       250        260        270        280        290        300 
APGRRLVLGG VEFEGDGLLG HSDADVCAHA IGDAILGAAG LGDLGRHFPD TDPRWKGVSS 

       310        320        330        340        350        360 
LALLREIAAK AAERGWRVGN CDVTLAAKRP KIAPRAEEMR ARLAGALGIS PAQVNVKATT 

       370        380 
GEGMGFVGRE EGVAAHAIAL LVRAAG

Q2IQG8 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