Reviewed, UniProtKB/Swiss-Prot Q2NAE1 (ISPDF_ERYLH)

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:	ELI_06290

Organism

Erythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]

Taxonomic identifier

314225 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter

Protein attributes

Sequence length	386 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 – 386	386	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292851
Regions
	Region	1 – 226	226	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	227 – 386	160	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	22	1	Transition state stabilizer By similarity
	Site	29	1	Transition state stabilizer By similarity
	Site	157	1	Positions MEP for the nucleophilic attack By similarity
	Site	212	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)
	Q2NAE1-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 41D3E50441D1CE2E	FASTA	386	40,308
	10 20 30 40 50 60 MATPSPLPSF AAIVVAAGKG LRAGQPVPKQ FATWRGKPVL RHSVESLRAA GADPIVVAIP 70 80 90 100 110 120 DHAGDVAAKA LDGITEVVFV TGGQTRQDSV RAALERLSSV PPERVLIHDA ARAILPTPVI 130 140 150 160 170 180 ERVLHGLDES GGAIPVLPVV DSLAVAAGER MADKADRESL RRVQTPQGFR FSDILAAHRA 190 200 210 220 230 240 WTGATDAGDD AQVLMAHGGD IALVEGDEAL KKLTFAEDFM ADLLPVRVGT GFDVHKLEAG 250 260 270 280 290 300 EELWLGGIRL EHDKGLAGHS DADVALHAIV DALLGAIGKG DIGDHFPPSD PQWKGAASSA 310 320 330 340 350 360 FIEHAAKLVD EAGYRVGNID LTIICEAPRI GPHRDAMGQR IAELLATSPD AISVKATTTE 370 380 KLGFTGRGEG IAAQAAATVV RKDTPA

References

[1]	Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S., Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000157 Genomic DNA. Translation: ABC63350.1.
RefSeq	YP_458147.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3871177.
GenomeReviews	Gene locus ELI_06290 in contig CP000157_GR.
KEGG	eli:ELI_06290.
NMPDR	fig|314225.3.peg.1798.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q2NAE1. IVLIHDA.
Enzyme and pathway databases
BioCyc	ELIT314225:ELI_06290-MON.
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_ERYLH

Accession

Primary (citable) accession number: Q2NAE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	February 7, 2006
Last modified:	June 16, 2009
This is version 18 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)