Q6ARN9 (ISPDF_DESPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional enzyme IspD/IspF

Including the following 2 domains:

1. 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. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
   Short name=MECDP-synthase
   Short name=MECPS
   EC=4.6.1.12

Gene names

Name:	ispDF
Ordered Locus Names:	DP0257

Organism

Desulfotalea psychrophila [Complete proteome] [HAMAP]

Taxonomic identifier

84980 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfobacterales › Desulfobulbaceae › Desulfotalea

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
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. HAMAP MF_01520
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. HAMAP MF_01520
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.
Sequence caution	The sequence CAG34986.1 differs from that shown. Reason: Erroneous initiation.

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: InterPro
Molecular function	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: EC 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: EC 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 – 386	386	Bifunctional enzyme IspD/IspF HAMAP MF_01520		PRO_0000075665
Regions
	Region	1 – 231	231	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	232 – 386	155	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	238	1	Divalent metal cation By similarity
	Metal binding	240	1	Divalent metal cation By similarity
	Metal binding	272	1	Divalent metal cation By similarity
	Site	16	1	Transition state stabilizer By similarity
	Site	23	1	Transition state stabilizer By similarity
	Site	153	1	Positions MEP for the nucleophilic attack By similarity
	Site	207	1	Positions MEP for the nucleophilic attack By similarity
	Site	264	1	Transition state stabilizer By similarity
	Site	363	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6ARN9 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 7100DD79827735E6	FASTA	386	41,971
	10 20 30 40 50 60 MKNGAVIIPA AGSGTRMKLD YPKQYHAVAG TPIIVHTIRA FNKHPCIAKI ILVVPQDHLE 70 80 90 100 110 120 ESKALLQKYQ LENISIVTGG ARRQDSVLRG LQEVPESIDI VLVHDGARPM VSAELISRCY 130 140 150 160 170 180 KGAQQYGAVI AAVPVKDTLK RGAGRIVTGT VDREGLWQAQ TPQAARKALL VKAFKENGMR 190 200 210 220 230 240 NVTDESTLLE GVGIPVTLIE GSETNIKITR PEDLILAENF LREKKEPMQK IRIGHGFDAH 250 260 270 280 290 300 QLVEKRRLIL GGVEIPYHLG LAGHSDADVL VHALCDALLG AIGAGDIGRH FPDSSDAFKD 310 320 330 340 350 360 IYSIRLLESV MQKVGELNYK IGNADISVIC QAPKLAPYLK QMQEIIATSC ACQISDINIK 370 380 ATTTEKMGYT GRGEGISCHA VVLLQQ

References

[1]

"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments." Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P. Environ. Microbiol. 6:887-902(2004) [PubMed: 15305914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR522870 Genomic DNA. Translation: CAG34986.1. Different initiation.
RefSeq	YP_063993.1. NC_006138.1.
3D structure databases
ProteinModelPortal	Q6ARN9.
SMR	Q6ARN9. Positions 231-386.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2946316.
GenomeReviews	Gene locus DP0257 in contig CR522870_GR.
KEGG	dps:DP0257.
NMPDR	fig|177439.1.peg.257.
PATRIC	21710055. VBIDesPsy67261_0282.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672839.
OMA	IVLIHDA.
ProtClustDB	CLSK2764635.
Enzyme and pathway databases
BioCyc	DPSY177439:DP0257-MONOMER.
Family and domain databases
HAMAP	MF_01520. IspDF. [Tree]
InterPro	IPR023423. IpsF_dom. IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase. IPR020555. MECDP_synthase_CS. [Graphical view]
Gene3D	G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
KO	K12506.
Pfam	PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view]
SUPFAM	SSF69765. YgbB_synth. 1 hit.
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_DESPS

Accession

Primary (citable) accession number: Q6ARN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	June 26, 2007
Last modified:	January 25, 2012
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program