Reviewed, UniProtKB/Swiss-Prot Q2K8V5 (ISPDF_RHIEC)

Names and origin

Protein names

Recommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
              EC=2.7.7.60
        Alternative name(s):
            4-diphosphocytidyl-2C-methyl-D-erythritol synthase
            MEP cytidylyltransferase
              Short name=MCT
    2- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12

Gene names

Name:	ispDF
Ordered Locus Names:	RHE_CH01945

Organism

Rhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]

Taxonomic identifier

347834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_01520 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520
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. HAMAP MF_01520 Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Sequence similarities	In the N-terminal section; belongs to the ispD family. In the C-terminal section; belongs to the ispF family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding
Molecular function	Lyase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: HAMAP 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292859
Regions
	Region	1 – 246	246	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	247 – 406	160	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	253	1	Divalent metal cation By similarity
	Metal binding	255	1	Divalent metal cation By similarity
	Metal binding	287	1	Divalent metal cation By similarity
	Site	24	1	Transition state stabilizer By similarity
	Site	33	1	Transition state stabilizer By similarity
	Site	167	1	Positions MEP for the nucleophilic attack By similarity
	Site	224	1	Positions MEP for the nucleophilic attack By similarity
	Site	279	1	Transition state stabilizer By similarity
	Site	378	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2K8V5-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 44A00BC422A9197E	FASTA	406	43,763
	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

References

[1]

"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons." 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. Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed: 16505379] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000133 Genomic DNA. Translation: ABC90731.1.
RefSeq	YP_469458.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3893983.
GenomeReviews	Gene locus RHE_CH01945 in contig CP000133_GR.
KEGG	ret:RHE_CH01945.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2K8V5.
OMA	Q2K8V5. IVLIHDA.
Family and domain databases
HAMAP	MF_01520. [Tree]
InterPro	IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. [Graphical view]
Pfam	PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00453. ispD. 1 hit. TIGR00151. ispF. 1 hit.
PROSITE	PS01295. ISPD. 1 hit. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_RHIEC

Accession

Primary (citable) accession number: Q2K8V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	March 7, 2006
Last modified:	June 16, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)