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:	BQ04980

From

Bartonella quintana (Rochalimaea quintana)

[TaxID: 803]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toulouse;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).

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

BX897700; CAF25997.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_032176.1; -.

3D structure databases

ModBase

Q6G164.

Enzyme and pathway databases

BioCyc

BQUI283165:BQ04980-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.

Gene3D

G3DSA:3.30.1330.50; MECDP_synthase_core; 1.

Pfam

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

TIGRFAMs

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

PROSITE

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

Genome annotation databases

GeneID

2866390; -.

GenomeReviews

BX897700_GR; BQ04980.

KEGG

bqu:BQ04980; -.

NMPDR

fig|283165.1.peg.446; -.

Phylogenomic databases

HOGENOM

Q6G164; -.

Genome annotation databases

CMR

Q6G164; BQ04980.

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`	`1 391`	`391`	`Bifunctional enzyme ispD/ispF.`	`PRO_0000075657`
`REGION`	`1 230`	`230`	`2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.`
`REGION`	`231 391`	`161`	`2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.`
`METAL`	`237 237`		`Divalent metal cation (By similarity).`
`METAL`	`239 239`		`Divalent metal cation (By similarity).`
`METAL`	`271 271`		`Divalent metal cation (By similarity).`
`SITE`	`9 9`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`18 18`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`149 149`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`206 206`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`263 263`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`362 362`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 391 AA [This is the length of the unprocessed precursor]

Molecular weight: 43792 Da [This is the MW of the unprocessed precursor]

CRC64: E81E1DC69C3B2B75 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLAAGRGKRA GSLQKNPKQY RLLGQKPVIC HTVRCFCQHP AITTIILVIH PEDRQICEQA 

        70         80         90        100        110        120 
ITDFKEHLII VEGGNTRQIS TLRGLHALKK FKPKYVHIHD GARPFIENKL LEKIHTTVNH 

       130        140        150        160        170        180 
QEGVLPVLPV SDTLKRVNST HRVLETIPHT HLYSAQTPQC FPFERILAAH ERAMQTCKKE 

       190        200        210        220        230        240 
FTDDSAIAEW FGIPMHTIPG DSHNIKITWH EDFDTAHLYL KKKMQMFPDI RTGNGYDVHS 

       250        260        270        280        290        300 
FEEGTSLILC GIKIPFHKKL KGHSDADVAF HALTDALLAT QGAGDIGTHF LPSDPQWKNA 

       310        320        330        340        350        360 
PSEIFLRHAL EIIKQAGGRI ANVDITLIAE TPKIGPYRHT MTENLMNILS LSLDRISIKA 

       370        380        390 
TTNEKLGFIG REEGIAALAT ATVLYPGEIP K

Q6G164 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