Reviewed, UniProtKB/Swiss-Prot Q5FQD6 (ISPDF_GLUOX)

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:	GOX1669

Organism

Gluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP]

Taxonomic identifier

442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length	388 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 – 388	388	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000075667
Regions
	Region	1 – 227	227	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	228 – 388	161	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	15	1	Transition state stabilizer By similarity
	Site	28	1	Transition state stabilizer By similarity
	Site	154	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)
	Q5FQD6-1 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: B17DEBBD569D502B	FASTA	388	41,815
	10 20 30 40 50 60 MRIAALLLAA GRGRRFDASS QSGENSSKQF RMLRGKPVIR RAAEALLPHV DVLLPVGDDP 70 80 90 100 110 120 LLADSLEGLD ILPPVSGGAE RHDSVRNGLE ALAKLPEPPD LVLVHDGARP CVPAEVVQNV 130 140 150 160 170 180 INALKTHEGV IPAVAVIDTI KKAKDGIIVD TVPRDGLWRA QTPQGFRFGT LLELHRTHRD 190 200 210 220 230 240 ARTDDAALLE QAGHPVAIVE GSEDNIKLTV AEDLMRLEGV IDRNLLPRVG LGYDVHAFEE 250 260 270 280 290 300 GRKLILCGIE VPHTKGLAGH SDADVGIHTL CDAIYGALAE GDIGRHFPPS DNKWKDMDSA 310 320 330 340 350 360 RFLVHAGERI RERGGFLVNA DVTLICERPK IGPHAEAMRN RLADLLKVSV SRISVKATTS 370 380 ERLGFTGREE GIAATATVSI MVPDNGEA

References

[1]

"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans." Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U. Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 621H.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000009 Genomic DNA. Translation: AAW61410.1. Different initiation.
RefSeq	YP_192066.1.
3D structure databases
SMR	Q5FQD6. Positions 2-384.
ModBase	Search...
Genome annotation databases
GeneID	3249409.
GenomeReviews	Gene locus GOX1669 in contig CP000009_GR.
KEGG	gox:GOX1669.
NMPDR	fig|290633.1.peg.1611.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672839.
Enzyme and pathway databases
BioCyc	GOXY290633:GOX1669-MONOMER.
BRENDA	2.7.7.60. 3050. 4.6.1.12. 3050.
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]
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_GLUOX

Accession

Primary (citable) accession number: Q5FQD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	February 9, 2010
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)