Reviewed, UniProtKB/Swiss-Prot Q0BTD5 (ISPDF_GRABC)

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:	GbCGDNIH1_1019

Organism

Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]

Taxonomic identifier

391165 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

Protein attributes

Sequence length	376 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 – 376	376	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296745
Regions
	Region	1 – 219	219	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	220 – 376	157	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	226	1	Divalent metal cation By similarity
	Metal binding	228	1	Divalent metal cation By similarity
	Metal binding	260	1	Divalent metal cation By similarity
	Site	15	1	Transition state stabilizer By similarity
	Site	22	1	Transition state stabilizer By similarity
	Site	146	1	Positions MEP for the nucleophilic attack By similarity
	Site	199	1	Positions MEP for the nucleophilic attack By similarity
	Site	252	1	Transition state stabilizer By similarity
	Site	351	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0BTD5-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 40820CD0A8BE074F	FASTA	376	39,766
	10 20 30 40 50 60 MRIAAILVAG GSGSRFGSDI PKQFLPVGGK PLIRHGAERL SAKVDLLQPV GCADDIAPLL 70 80 90 100 110 120 QGLDHLPIVD GGKERQDSVR AGLEALVPYA PDIVLIHDAA RPYFPDHTIE DLIEALQIHD 130 140 150 160 170 180 GAIPAVPVAD TLKRAAGNII DSTVPREGLY RAQTPQAFKF SVLLALHRDH PGGATDDAAL 190 200 210 220 230 240 LDQAGHSVAL VPGAEDNIKV TYPADLARVE RSMSISMIPR IGTGYDVHAF ETGRKLILCG 250 260 270 280 290 300 IEVPHHQGLA GHSDADVGIH ALCDAIYGAL AEGDIGRHFP PTEASWKDAD SARFLRHAAE 310 320 330 340 350 360 RIAARGGFLA NADLTLICEK PKITPHAPAM IARLAELLGV SIDKISVKAT TSEKLGFTGR 370 EEGIAAQAAV IIMIPA

References

[1]

"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis." Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M. J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000394 Genomic DNA. Translation: ABI61917.1.
RefSeq	YP_744840.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4275844.
GenomeReviews	Gene locus GbCGDNIH1_1019 in contig CP000394_GR.
KEGG	gbe:GbCGDNIH1_1019.
NMPDR	fig|391165.8.peg.1020.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0BTD5.
OMA	Q0BTD5. IVLIHDA.
Family and domain databases
HAMAP	MF_01520. [Tree]
InterPro	IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. [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_GRABC

Accession

Primary (citable) accession number: Q0BTD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 19 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)