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:	bll4485

From

Bradyrhizobium japonicum

[TaxID: 375]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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

BA000040; BAC49750.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_771125.1; -.

3D structure databases

HSSP

P44815; 1JN1. [HSSP ENTRY / PDB]

ModBase

Q89LQ8.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL4485-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; 1.

Genome annotation databases

GeneID

1052654; -.

GenomeReviews

BA000040_GR; bll4485.

KEGG

bja:bll4485; -.

NMPDR

fig|224911.1.peg.4485; -.

Phylogenomic databases

HOGENOM

Q89LQ8; -.

Genome annotation databases

CMR

Q89LQ8; bll4485.

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`	`1 398`	`398`	`Bifunctional enzyme ispD/ispF.`	`PRO_0000075658`
`REGION`	`1 234`	`234`	`2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.`
`REGION`	`235 398`	`164`	`2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.`
`METAL`	`241 241`		`Divalent metal cation (By similarity).`
`METAL`	`243 243`		`Divalent metal cation (By similarity).`
`METAL`	`275 275`		`Divalent metal cation (By similarity).`
`SITE`	`19 19`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`26 26`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`156 156`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`213 213`	`1`	`Positions MEP for the nucleophilic attack (By similarity).`
`SITE`	`267 267`	`1`	`Transition state stabilizer (By similarity).`
`SITE`	`366 366`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 398 AA [This is the length of the unprocessed precursor]

Molecular weight: 42226 Da [This is the MW of the unprocessed precursor]

CRC64: 93E0A201CB315B6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKSQRTAVV LVAAGRGLRA GAGGPKQYRE IGGQPVIYRA MEAFSRHPDV FAVQPVVNPD 

        70         80         90        100        110        120 
DSAMFTAAVA GLKHEPPTNG GATRQASVLA GLEALAKHQP DIVLIHDAAR PFVSDGVISR 

       130        140        150        160        170        180 
AIDAASRTGA AIPVVPVTDT IKLTGASGNV EDTPDRARLR IAQTPQSFRF DVILEAHRRA 

       190        200        210        220        230        240 
AKDGRSDFTD DAAIAEWAGL TVATFEGDVA NMKLTTPEDF VREEARLAAQ LGDIRTGTGY 

       250        260        270        280        290        300 
DVHAFGEGDH VMICGVRVPH SKGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDAK 

       310        320        330        340        350        360 
WKGASSDQFL KYAIERVAQR GGRVANLEVT MICERPKIGP LRDTMRARIA EISGVDISRV 

       370        380        390 
AVKATTSERL GFTGREEGIA ATASATIRLP FNEKTWSV

Q89LQ8 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