Reviewed, UniProtKB/Swiss-Prot Q2G708 (ISPDF_NOVAD)

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:	Saro_1925

Organism

Novosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]

Taxonomic identifier

279238 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Novosphingobium

Protein attributes

Sequence length	386 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 – 386	386	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292857
Regions
	Region	1 – 230	230	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	231 – 386	156	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	237	1	Divalent metal cation By similarity
	Metal binding	239	1	Divalent metal cation By similarity
	Metal binding	271	1	Divalent metal cation By similarity
	Site	24	1	Transition state stabilizer By similarity
	Site	31	1	Transition state stabilizer By similarity
	Site	159	1	Positions MEP for the nucleophilic attack By similarity
	Site	214	1	Positions MEP for the nucleophilic attack By similarity
	Site	263	1	Transition state stabilizer By similarity
	Site	362	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2G708-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 716C422DEB3B7D17	FASTA	386	40,153
	10 20 30 40 50 60 MNSVPSLPGQ SVAAVVVAGG KGLRTGGPVP KQFVIWRGKP LLRHCVEALE AAGIAPIVVA 70 80 90 100 110 120 IPAGWDEAAT QALAGISMVR LVHGGATRQE SVKAALEVLE GDAPARVLIH DAARPDLPGS 130 140 150 160 170 180 VIERLLTALD KRTGAIPVLP VVDSMVRGSG DAMGETVARE DLYRVQTPQA FHYPAILAAH 190 200 210 220 230 240 RAWQGEALAG DDAQVAMRAA HEIALVEGDE ALRKVTFASD LEEQSMSVIP RTGMGFDVHR 250 260 270 280 290 300 LVEGEELWLC GVNIPHGKGL SGHSDADVAI HALVDALLGA IAAGDIGDHF PPSDPQWKGA 310 320 330 340 350 360 SSDRFLAHAG TLVTEAGYRI ANVDVTIICE APKIGPHKAA MRETLARILG IDSALVSVKA 370 380 TTTERLGLTG RGEGIAAQAV ATVVSG

References

[1]

"Complete sequence of Novosphingobium aromaticivorans DSM 12444." 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., Kyrpides N., Ivanova N. , Fredrickson J., Balkwill D., Romine M.F., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000248 Genomic DNA. Translation: ABD26365.1.
RefSeq	YP_497199.1.
3D structure databases
SMR	Q2G708. Positions 11-384.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2G708.
Genome annotation databases
GeneID	3917148.
GenomeReviews	Gene locus Saro_1925 in contig CP000248_GR.
KEGG	nar:Saro_1925.
NMPDR	fig|48935.1.peg.896.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1211.
HOGENOM	HBG672839.
OMA	IVLIHDA.
PhylomeDB	Q2G708.
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]
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_NOVAD

Accession

Primary (citable) accession number: Q2G708

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	March 21, 2006
Last modified:	February 9, 2010
This is version 27 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)