Reviewed, UniProtKB/Swiss-Prot Q07MZ2 (ISPDF_RHOP5)

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:	RPE_2755

Organism

Rhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP]

Taxonomic identifier

316055 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
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. HAMAP MF_01520
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. HAMAP MF_01520
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520 Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate 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 – 398	398	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296753
Regions
	Region	1 – 234	234	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	235 – 398	164	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	241	1	Divalent metal cation By similarity
	Metal binding	243	1	Divalent metal cation By similarity
	Metal binding	275	1	Divalent metal cation By similarity
	Site	19	1	Transition state stabilizer By similarity
	Site	26	1	Transition state stabilizer By similarity
	Site	156	1	Positions MEP for the nucleophilic attack By similarity
	Site	213	1	Positions MEP for the nucleophilic attack By similarity
	Site	267	1	Transition state stabilizer By similarity
	Site	366	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07MZ2-1 [UniParc]. Last modified October 31, 2006. Version 1. Checksum: 70BFCC5CAED33012	FASTA	398	42,313
	10 20 30 40 50 60 MANSRRTAAI IVAGGRGLRA GGGGPKQYRT LAGQPVIYRS MQPFCTHPDV FAVQPVTSPD 70 80 90 100 110 120 DIALFEQAVA GLTHRPPANG GATRQQSVYS GLEALAKDAP DIVLIHDAAR AFVDAALISR 130 140 150 160 170 180 AIVAAQRTGA AVPTIPVTDT IKQVNGTNDV EATPDRATLR IAQTPQAFRY DVILEAHRRA 190 200 210 220 230 240 AREGRDDFTD DAAIAEWAGL TVATFEGDAA NMKLTTPEDF VREESRLAAL LGDIRTGTGY 250 260 270 280 290 300 DVHAFGDGDH VWLCGLKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPTDPQ 310 320 330 340 350 360 WKGAASDKFL KYAIDRVHAR GGRIANLEVT MICERPKIGP LREAMRERIA EITGLPVSRI 370 380 390 AVKATTSERL GFTGREEGIA ATACATIRLP WGPNGLSG

References

[1]

"Complete sequence of Rhodopseudomonas palustris BisA53." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., Richardson P. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000463 Genomic DNA. Translation: ABJ06692.1.
RefSeq	YP_781672.1.
3D structure databases
SMR	Q07MZ2. Positions 6-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q07MZ2.
Genome annotation databases
GeneID	4360437.
GenomeReviews	Gene locus RPE_2755 in contig CP000463_GR.
KEGG	rpe:RPE_2755.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1211.
HOGENOM	HBG672839.
OMA	IVLIHDA.
Family and domain databases
HAMAP	MF_01520. IspDF. [Tree]
InterPro	IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. IPR020555. MECDP_synthase_CS. [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_RHOP5

Accession

Primary (citable) accession number: Q07MZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	October 31, 2006
Last modified:	February 9, 2010
This is version 23 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)