Reviewed, UniProtKB/Swiss-Prot Q2RTS1 (ISPDF_RHORT)

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:	Rru_A1674

Organism

Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Complete proteome] [HAMAP]

Taxonomic identifier

269796 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length	384 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 – 384	384	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292860
Regions
	Region	1 – 227	227	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	228 – 384	157	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	234	1	Divalent metal cation By similarity
	Metal binding	236	1	Divalent metal cation By similarity
	Metal binding	268	1	Divalent metal cation By similarity
	Site	16	1	Transition state stabilizer By similarity
	Site	23	1	Transition state stabilizer By similarity
	Site	153	1	Positions MEP for the nucleophilic attack By similarity
	Site	207	1	Positions MEP for the nucleophilic attack By similarity
	Site	260	1	Transition state stabilizer By similarity
	Site	359	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2RTS1-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: C50CD5FA4F5EF47C	FASTA	384	40,287
	10 20 30 40 50 60 MAKVAALIVA AGRGKRFGGD LPKQYQTLGG RPILRHTLAR FAAHPDVALV RAIIHPEDRD 70 80 90 100 110 120 LYGAAAHGLA TLLDAVEGGA ERQDSVRLGL ESLTDVAPDY VLIHDGARPL VDGALIDRVI 130 140 150 160 170 180 AALADHPGAI PALAVADTLK RGAGGMIGQT VDRAGLWRAQ TPQGFRYDAI LAAHRAQAGT 190 200 210 220 230 240 MLTDDAAVLE AAGGAVALVD GAEDNAKITT FADLERAERL FRGEGEQRIG SGFDVHRLGP 250 260 270 280 290 300 GDFVTLNGIR IPHSHGLVGH SDADAPMHAL TDALLGCLNA GDIGRHFPPS DMRWKGADSA 310 320 330 340 350 360 IFLRHAAALI TALGGRILNV DITILCEQPK IGPHRARMSA RLAEILEISA TRVAVKATTT 370 380 EELGFTGRGE GIAAQATALI TLPF

References

[1]

"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000230 Genomic DNA. Translation: ABC22474.1.
RefSeq	YP_426761.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3835094.
GenomeReviews	Gene locus Rru_A1674 in contig CP000230_GR.
KEGG	rru:Rru_A1674.
NMPDR	fig|1085.1.peg.2251.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2RTS1.
OMA	Q2RTS1. IVLIHDA.
Enzyme and pathway databases
BioCyc	RRUB269796:RRU_A1674-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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_RHORT

Accession

Primary (citable) accession number: Q2RTS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 21 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)