Reviewed, UniProtKB/Swiss-Prot A8LKV5 (ISPDF_DINSH)

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:	Dshi_1577

Organism

Dinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]

Taxonomic identifier

398580 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Dinoroseobacter

Protein attributes

Sequence length	400 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 – 400	400	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000333305
Regions
	Region	1 – 244	244	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	245 – 400	156	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	251	1	Divalent metal cation By similarity
	Metal binding	253	1	Divalent metal cation By similarity
	Metal binding	285	1	Divalent metal cation By similarity
	Site	35	1	Transition state stabilizer By similarity
	Site	42	1	Transition state stabilizer By similarity
	Site	169	1	Positions MEP for the nucleophilic attack By similarity
	Site	222	1	Positions MEP for the nucleophilic attack By similarity
	Site	277	1	Transition state stabilizer By similarity
	Site	376	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8LKV5-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 23F281F018DD6475	FASTA	400	42,011
	10 20 30 40 50 60 MSHRVLGTER ISPREEHVLT PNVTAILVAA GRGTRAGGGL AKQWRPLGAR RVIDWTLAAF 70 80 90 100 110 120 DRATQVSELL VVLHPEDMDL AATLTAAKPL RCVSGGATRS ASVACALAAV ADPEAIVLIH 130 140 150 160 170 180 DAARPVVSAD LIARVVAGVI ETGAAAPALP VVDALWTGAG DRVTGMQPRD GLYRAQTPQG 190 200 210 220 230 240 FHAGAIRDAH AAATGAAADD VEIARAAGMP VAIVAGDEQN FKITYPQDFA RAAALLKERD 250 260 270 280 290 300 KMDIRTGNGY DVHRFGTGDA VILCGVEVPH DRALMGHSDA DVGMHAVTDA IYGALGDGDI 310 320 330 340 350 360 GQHFPPSDPQ WKGAASEIFL RHAVALAAER GYTITHMDCT LVCERPKIGP YHAVMKAKMS 370 380 390 400 ELMGLQPDQV SVKATTSERL GFTGREEGIA ALATVTLVRT

References

[1]

"Complete sequence of chromosome of Dinoroseobacter shibae DFL 12." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Richardson P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000830 Genomic DNA. Translation: ABV93319.1.
RefSeq	YP_001532920.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5712721.
GenomeReviews	Gene locus Dshi_1577 in contig CP000830_GR.
KEGG	dsh:Dshi_1577.
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. 1 hit. PS01350. ISPF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ISPDF_DINSH

Accession

Primary (citable) accession number: A8LKV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 4, 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)