Reviewed, UniProtKB/Swiss-Prot Q08113 (ISPDF_RHOCA)

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

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	379 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	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 – 379	379	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000075675
Regions
	Region	1 – 223	223	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	224 – 379	156	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	230	1	Divalent metal cation By similarity
	Metal binding	232	1	Divalent metal cation By similarity
	Metal binding	264	1	Divalent metal cation By similarity
	Site	15	1	Transition state stabilizer By similarity
	Site	22	1	Transition state stabilizer By similarity
	Site	146	1	Positions MEP for the nucleophilic attack By similarity
	Site	199	1	Positions MEP for the nucleophilic attack By similarity
	Site	256	1	Transition state stabilizer By similarity
	Site	355	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08113-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4A1A4377FBC34628	FASTA	379	39,511
	10 20 30 40 50 60 MTVAVIIVAA GRGTRAGEGL PKQWRDLAGR PVLAQTVAAF AGLGRILVVL HPDDMGLGMD 70 80 90 100 110 120 LLGGSVVLVA GGSTRSESVK NALEALEGSD VTRVLIHDGA RPLVPASVTA AVLAALETTP 130 140 150 160 170 180 GAAPALAVTD ALWRGEAGLV AGTQDREGLY RAQTPQGFRF PEILAAHRAH PGGAADDVEV 190 200 210 220 230 240 ARHAGLSVAI VPGHEDNLKI TYAPDFARAE AILRERKGLT MDVRLGNGYD VHAFCEGDHV 250 260 270 280 290 300 VLCGVKVPHV KALLGHSDAD VGMHALTDAI YGALAEGDIG RHFPPSDPQW KGAASWIFLD 310 320 330 340 350 360 HAAKLAKSRG FRIGNADVTL ICERPKVGPH AVAMAAELAR IMEIEPSRVS VKATTSERLG 370 FTGREEGIAS IATVTLIGA

References

[1]

"Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC operon in Rhodobacter capsulatus." Foster-Hartnett D., Cullen P.J., Gabbert K.K., Kranz R.G. Mol. Microbiol. 8:903-914(1993) [PubMed: 8355615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X72382 Genomic DNA. Translation: CAA51072.1.
PIR	S34980.
3D structure databases
HSSP	HSSP built from PDB template 1JN1 based on UniProtKB P44815.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.7.60. 567. 4.6.1.12. 567.
Family and domain databases
HAMAP	MF_01520. [Tree]
InterPro	IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. [Graphical view]
Gene3D	G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
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_RHOCA

Accession

Primary (citable) accession number: Q08113

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 5, 2009
This is version 56 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)