Reviewed, UniProtKB/Swiss-Prot Q28Q60 (ISPDF_JANSC)

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:	Jann_2235

Organism

Jannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]

Taxonomic identifier

290400 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Jannaschia

Protein attributes

Sequence length	382 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 – 382	382	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292853
Regions
	Region	1 – 226	226	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	227 – 382	156	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	233	1	Divalent metal cation By similarity
	Metal binding	235	1	Divalent metal cation By similarity
	Metal binding	267	1	Divalent metal cation By similarity
	Site	20	1	Transition state stabilizer By similarity
	Site	27	1	Transition state stabilizer By similarity
	Site	152	1	Positions MEP for the nucleophilic attack By similarity
	Site	205	1	Positions MEP for the nucleophilic attack By similarity
	Site	259	1	Transition state stabilizer By similarity
	Site	358	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q28Q60-1 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 5078CD9618664D67	FASTA	382	40,213
	10 20 30 40 50 60 MEKPAQRATA IIVAAGRGIR AGGGEPKQWR RIAGRSIVEW SVNRFAAHHA GFDVVLVIHP 70 80 90 100 110 120 DDEWRLNGLD LPTTLRVVHG GDSRAASVKA GLAVCCDAGH VLIHDVARPC VSLAVIQSVL 130 140 150 160 170 180 DATRAGGAAA PALPVTDALW RGDTHVSGTQ NRDGLWRAQT PQGFDVSAIR AAHAAHDGTA 190 200 210 220 230 240 ADDVEVARLA GIDVAIVPGD EANLKITGPE DFARAEALLT GGDMDIRVGN GFDVHRFGPG 250 260 270 280 290 300 DQVWLCGISV PHTRGLQGHS DADVGLHTLT DAIYGALAEG DIGTHFPPSD PQWKDAESHI 310 320 330 340 350 360 FLTHAVELAA NRGFSITNAD LTLICEQPKI GPVASAMRAR VADLLRIDVA RVSVKATTSE 370 380 RLGFTGREEG IAALATITLV AR

References

[1]

"Complete sequence of chromosome of Jannaschia sp. CCS1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000264 Genomic DNA. Translation: ABD55152.1.
RefSeq	YP_510177.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q28Q60.
Genome annotation databases
GeneID	3934689.
GenomeReviews	Gene locus Jann_2235 in contig CP000264_GR.
KEGG	jan:Jann_2235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q28Q60.
OMA	IVLIHDA.
Enzyme and pathway databases
BioCyc	JSP290400:JANN_2235-MON.
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_JANSC

Accession

Primary (citable) accession number: Q28Q60

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	April 4, 2006
Last modified:	November 3, 2009
This is version 20 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)