Reviewed, UniProtKB/Swiss-Prot Q0APQ6 (ISPDF_MARMM)

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:	Mmar10_1439

Organism

Maricaulis maris (strain MCS10) [Complete proteome] [HAMAP]

Taxonomic identifier

394221 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Maricaulis

Protein attributes

Sequence length	383 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 – 383	383	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296749
Regions
	Region	1 – 226	226	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	227 – 383	157	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	15	1	Transition state stabilizer By similarity
	Site	22	1	Transition state stabilizer By similarity
	Site	152	1	Positions MEP for the nucleophilic attack By similarity
	Site	206	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)
	Q0APQ6-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: F5F0A75DABC804D4	FASTA	383	40,316
	10 20 30 40 50 60 MKIAAVIVAA GRGERAGGGV PKQYRRLGGF FVLTHTLLRL LHREVFDSII VVVNPADADH 70 80 90 100 110 120 IAAVEAELDI KLDTVPGGAT RTASVRAGLE RARDLGLDAV MIHDAARPFL GDALIDRLVK 130 140 150 160 170 180 ALADHPAVIP ALPVADALFR GGDARMGDPV SRDGLYAAQT PQAFHLAPLL KAYARLGDTA 190 200 210 220 230 240 LPDDAAVIRA AGGEVALVPG EAENFKLTTR ADFERAERQI MSETITVTGQ GYDVHRLEPA 250 260 270 280 290 300 DVMWLCGVEI RAGLGLIGHS DADAGLHALT DAVLGAAGAG DIGQHFPPSD PQWKGAASDA 310 320 330 340 350 360 FLLHAIKLLK QVGGELVHAD ITLIAERPKI GPHRDAMRAR VAELTGLPEK RVNIAATTTE 370 380 KLGFTGRGEG LAAQAIVTAR LTT

References

[1]

"Complete sequence of Maricaulis maris MCS10." 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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000449 Genomic DNA. Translation: ABI65731.1.
RefSeq	YP_756669.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0APQ6.
Genome annotation databases
GeneID	4285678.
GenomeReviews	Gene locus Mmar10_1439 in contig CP000449_GR.
KEGG	mmr:Mmar10_1439.
NMPDR	fig|394221.5.peg.1404.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0APQ6.
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_MARMM

Accession

Primary (citable) accession number: Q0APQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	October 17, 2006
Last modified:	November 3, 2009
This is version 23 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)