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:	Atu1443
	ORFNames:	AGR_C_2659

From

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

[TaxID: 176299]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066804; PubMed=11743193 [NCBI, ExPASy, EBI, Israel, Japan]
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W.;
"The genome of the natural genetic engineer Agrobacterium tumefaciens C58.";
Science 294:2317-2323(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066803; PubMed=11743194 [NCBI, ExPASy, EBI, Israel, Japan]
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58.";
Science 294:2323-2328(2001).

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

AE007869; AAK87234.2; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A97535; A97535.
AC2754; AC2754.

RefSeq

NP_354449.2; -.

3D structure databases

HSSP

P36663; 1JY8. [HSSP ENTRY / PDB]

ModBase

Q8UFF4.

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

Q8UFF4.

Genome annotation databases

GeneID

1133481; -.

GenomeReviews

AE007869_GR; Atu1443.

KEGG

atc:AGR_C_2659; -.
atu:Atu1443; -.

Phylogenomic databases

HOGENOM

Q8UFF4; -.

Genome annotation databases

CMR

Q8UFF4; Atu1443.

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`	`1 400`	`400`	`Bifunctional enzyme ispD/ispF.`	`PRO_0000075655`
`REGION`	`1 240`	`240`	`2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.`
`REGION`	`241 400`	`160`	`2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.`
`METAL`	`247 247`		`Divalent metal cation (By similarity).`
`METAL`	`249 249`		`Divalent metal cation (By similarity).`
`METAL`	`281 281`		`Divalent metal cation (By similarity).`
`SITE`	`20 20`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`29 29`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`162 162`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`219 219`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`273 273`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`372 372`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 42361 Da [This is the MW of the unprocessed precursor]

CRC64: CD11455C9D35D851 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQESTMKFGI VIVAAGRGER AGSPEEGPKQ YRPIGGRAVI EHTLATFLRW NDACPIVVVS 

        70         80         90        100        110        120 
HADDAALLSP ILARLDAGER ITTVTGGATR QQSVLAGLEA LSSHGLTHVM IHDAVRPFVA 

       130        140        150        160        170        180 
ADMLERIAAL HRAGAGGVLP ALPVTDTLKR GLEDRVVETV SRQGLYAAQT PQSFSYSDIL 

       190        200        210        220        230        240 
DAHRAAAASG KTDFTDDASI AEWTGLTVTL TEGSVDNVKL TLKRDIAMAD EKLSHALPDV 

       250        260        270        280        290        300 
RTGNGYDVHQ LEAGDGVTLC GIFIEHDQRL KGHSDADVAL HALTDALLAT CGAGDIGDHF 

       310        320        330        340        350        360 
PPSDPQWKGA ASRIFLEHAA KVVRDNGGTI MNADVSLIAE APRIGPHRQA MREALSDMLG 

       370        380        390        400 
IALERCSVKA TTNETIGFVG RREGIAAIAT ATVVYQGRPL

Q8UFF4 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