Reviewed, UniProtKB/Swiss-Prot Q1QM99 (ISPDF_NITHX)

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:	Nham_1834

Organism

Nitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]

Taxonomic identifier

323097 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Nitrobacter

Protein attributes

Sequence length	403 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 – 403	403	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292856
Regions
	Region	1 – 234	234	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	235 – 403	169	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)
	Q1QM99-1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: C18698298DDC8335	FASTA	403	42,798
	10 20 30 40 50 60 MPTSKRTAAI IVAAGRGLRA GTGGPKQYRT IAGRTVIARA MEAFCDHPDV FAVQPVLNPD 70 80 90 100 110 120 DLAMFNQAVA GFRYRPPANG GATRQASVHA GLEALAADAP DIVLIHDAAR PFATPALIRR 130 140 150 160 170 180 AIEATDITGA AVPVIPVTDT IKQVDASGAV NATPDRAKLR IAQTPQAFRF DVILDAHRRA 190 200 210 220 230 240 ARDGRDDFTD DAALAEWVGL TVATFEGDAA NMKLTTPEDF VREEARLAAM LGDIRTGTGY 250 260 270 280 290 300 DVHAFGDGDH VMLCGVKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDPQ 310 320 330 340 350 360 WKGAASDKFL KYAVDRVAAR GGRIANLEVT MICERPKIGP LRDTMRARIA EITGVAISRI 370 380 390 400 AVKATTSERL GFTGREEGIA TTASATVRLP WNDSDQEDKG WST

References

[1]

"Complete sequence of chromosome of Nitrobacter hamburgensis X14." 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., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000319 Genomic DNA. Translation: ABE62648.1. Different initiation.
RefSeq	YP_577108.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4033011.
GenomeReviews	Gene locus Nham_1834 in contig CP000319_GR.
KEGG	nha:Nham_1834.
NMPDR	fig|323097.3.peg.3209.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1QM99.
Enzyme and pathway databases
BioCyc	NHAM323097:NHAM_1834-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_NITHX

Accession

Primary (citable) accession number: Q1QM99

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	May 5, 2009
This is version 18 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)