Reviewed, UniProtKB/Swiss-Prot A5VQP4 (ISPDF_BRUO2)

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:	BOV_1078

Organism

Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]

Taxonomic identifier

444178 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	409 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 – 409	409	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000315550
Regions
	Region	1 – 248	248	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	249 – 409	161	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	255	1	Divalent metal cation By similarity
	Metal binding	257	1	Divalent metal cation By similarity
	Metal binding	289	1	Divalent metal cation By similarity
	Site	27	1	Transition state stabilizer By similarity
	Site	36	1	Transition state stabilizer By similarity
	Site	167	1	Positions MEP for the nucleophilic attack By similarity
	Site	224	1	Positions MEP for the nucleophilic attack By similarity
	Site	281	1	Transition state stabilizer By similarity
	Site	380	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5VQP4-1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: F10132EC33C4CF3C	FASTA	409	43,720
	10 20 30 40 50 60 MQAQSLAEVT VISKAAAVIV AAGRGERAGQ SAEGPKQYRL IGAEAVLART LRAFTDCPLI 70 80 90 100 110 120 GTIAVVIHPD DHALYRRAVP EKHENVILVT GGPTRQESTR LGLLALKDEA PQYVLIHDGV 130 140 150 160 170 180 RPFIGQDLLE RIIANLTPDN GVLPALAVSD TLKRAAADGM VETTISRTGL FAAQTPQAFP 190 200 210 220 230 240 YAPILDAHEK AFAINRTDFT DDAAIAEWQE IAVRIIEGSA DNTKLTWAKD IEMADKRLRQ 250 260 270 280 290 300 DHAVFPDIRT GNGYDVHSFE PGDHVTLCGV KIPHEAKLNG HSDADVALHA LTDALLATRG 310 320 330 340 350 360 AGDIGTHFPP SDPQWKGAAS RIFIEHAAKI VREAGGRIAN VDVTLISEAP KIGPHRAAMT 370 380 390 400 QALCDMLGIA ADRVSIKATT NEKLGFVGRR EGIAAIATAT VIYPGEVPE

References

[1]	Paulsen I. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000708 Genomic DNA. Translation: ABQ60504.1. Different initiation.
RefSeq	YP_001259041.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5201895.
GenomeReviews	Gene locus BOV_1078 in contig CP000708_GR.
KEGG	bov:BOV_1078.
TIGR	BOV_1078.
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_BRUO2

Accession

Primary (citable) accession number: A5VQP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	September 22, 2009
This is version 14 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)