Reviewed, UniProtKB/Swiss-Prot Q214R1 (ISPDF_RHOPB)

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:	RPC_2575

Organism

Rhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]

Taxonomic identifier

316056 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	398 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 – 398	398	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296754
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)
	Q214R1-1 [UniParc]. Last modified April 18, 2006. Version 1. Checksum: 012B98D1DC73F235	FASTA	398	42,099
	10 20 30 40 50 60 MSNSKRTAAI IVAGGRGLRA GAGGPKQYRS LAGQPVIFRA MQPFCTHAEI FAVQPVTSPD 70 80 90 100 110 120 DAEMFKLAVA GLNYQPPAPG GATRQGSVRA GLEALAADAP DIVLIHDAAR PFVDAALISR 130 140 150 160 170 180 AIVAAQITGA AVPTIAVTDT IKQINAQGDV VATPDRARLR IAQTPQAFRF DVILEAHRRA 190 200 210 220 230 240 AREGRDDFTD DAAIAEWAGL TVATFEGDVA NMKLTTPEDF VREESRLGAL LGDIRTGTGY 250 260 270 280 290 300 DVHAFGDGDH VWLCGLKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPTDPQ 310 320 330 340 350 360 WKGAASDKFL KYAVDRVTAR GGRIANLEVT MICERPKIGP LREPMRQRIA EITGLPVARI 370 380 390 AVKATTSERL GFTGREEGIA ATASATLRLP WGTNGLAD

References

[1]

"Complete sequence of Rhodopseudomonas palustris BisB18." 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., Anderson I., Oda Y., Harwood C.S., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000301 Genomic DNA. Translation: ABD88125.1.
RefSeq	YP_532444.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3970914.
GenomeReviews	Gene locus RPC_2575 in contig CP000301_GR.
KEGG	rpc:RPC_2575.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q214R1.
OMA	Q214R1. IVLIHDA.
Enzyme and pathway databases
BioCyc	RPAL316056:RPC_2575-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_RHOPB

Accession

Primary (citable) accession number: Q214R1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	April 18, 2006
Last modified:	June 16, 2009
This is version 19 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)