Reviewed, UniProtKB/Swiss-Prot Q2IW23 (ISPDF_RHOP2)

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:	RPB_2885

Organism

Rhodopseudomonas palustris (strain HaA2) [Complete proteome] [HAMAP]

Taxonomic identifier

316058 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	401 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 – 401	401	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296756
Regions
	Region	1 – 234	234	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	235 – 401	167	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)
	Q2IW23-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 51DF150C2A2EBF9C	FASTA	401	42,361
	10 20 30 40 50 60 MQKPPRTAAI IVAAGRGLRA GAGGPKQYRT LAGRPVIARA LQPFCTHPEV FAVQPVTNPD 70 80 90 100 110 120 DTATFNEAVA GLDFRPAVGG GATRQASVRA GLEALAELNP DIVLIHDAAR PFVTPDLISR 130 140 150 160 170 180 AIVAAGQTGA ALPVIAVNDT VKQVDAEGCV VATPDRAQLR IAQTPQAFRF DVILDAHRRA 190 200 210 220 230 240 ARDGRDDFTD DAAIAEWAGL TVSTFEGDAA NMKLTTPEDF SREESRLTAA LGDIRTGTGY 250 260 270 280 290 300 DVHAFGDGDH VWLCGLKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPTDPQ 310 320 330 340 350 360 WKGAASDKFL KYAVDRVAAR GGRIANLEVT MICERPKIGP LRDPMRQRIA EITGVPVSRV 370 380 390 400 AVKATTSERL GFTGREEGIA ATASATIRLP WSPWGAEGQA S

References

[1]

"Complete sequence of Rhodopseudomonas palustris HaA2." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A. , Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000250 Genomic DNA. Translation: ABD07587.1.
RefSeq	YP_486498.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3910679.
GenomeReviews	Gene locus RPB_2885 in contig CP000250_GR.
KEGG	rpb:RPB_2885.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2IW23.
OMA	Q2IW23. IVLIHDA.
Enzyme and pathway databases
BioCyc	RPAL316058:RPB_2885-MON.
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_RHOP2

Accession

Primary (citable) accession number: Q2IW23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	March 7, 2006
Last modified:	June 16, 2009
This is version 20 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)