Reviewed, UniProtKB/Swiss-Prot A6Q2K0 (ISPDF_NITSB)

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:	NIS_0595

Organism

Nitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]

Taxonomic identifier

387092 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Nitratiruptor

Protein attributes

Sequence length	373 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 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 – 373	373	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000315553
Regions
	Region	1 – 213	213	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	214 – 373	160	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	219	1	Divalent metal cation By similarity
	Metal binding	221	1	Divalent metal cation By similarity
	Metal binding	253	1	Divalent metal cation By similarity
	Site	16	1	Transition state stabilizer By similarity
	Site	23	1	Transition state stabilizer By similarity
	Site	140	1	Positions MEP for the nucleophilic attack By similarity
	Site	192	1	Positions MEP for the nucleophilic attack By similarity
	Site	245	1	Transition state stabilizer By similarity
	Site	344	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6Q2K0-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: E3E072565A391C35	FASTA	373	41,963
	10 20 30 40 50 60 MSDLTLVLLG AGNSSRFGLD VKKQWLWCGN EPLWLYVTNR FTDMFPFHDV VITAHPKEIP 70 80 90 100 110 120 FYKKFCHHTI VKGADTRQQS LLNALEMVKT PYVLVSDIAR PCIQKEVVQK IIDNRSKAAC 130 140 150 160 170 180 IVPYIQPADT VVYKNETIDR NEVKLIQTPQ LSSTDILRKA LTQGKEFTDE SSAIQALGEK 190 200 210 220 230 240 VFYILGNRKQ HKLTYKEDMK LLNCLQKPSA TKRIGNGLDV HAFCEDRKLY LCGIEIPYDK 250 260 270 280 290 300 GLAGHSDADV AIHALIDALL GAAGFGDIGE LFPDSDETYK DIDSKKLLCE TVRLLRACGF 310 320 330 340 350 360 VIEHVDLTIV AQNPKIGPFK EKMKESLHDL LQIPYHLINL KATTTEHLGF VGRNEGIAAM 370 ATATLHYFDW SEI

References

[1]

"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens." Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K. Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed: 17615243] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP009178 Genomic DNA. Translation: BAF69709.1.
RefSeq	YP_001356066.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A6Q2K0.
Genome annotation databases
GeneID	5360385.
GenomeReviews	Gene locus NIS_0595 in contig AP009178_GR.
KEGG	nis:NIS_0595.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IVLIHDA.
Family and domain databases
HAMAP	MF_01520. [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. False negative. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_NITSB

Accession

Primary (citable) accession number: A6Q2K0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 21, 2007
Last modified:	November 3, 2009
This is version 15 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)