Reviewed, UniProtKB/Swiss-Prot Q1MR76 (ISPDF_LAWIP)

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:	LI0446

Organism

Lawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP]

Taxonomic identifier

363253 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Lawsonia

Protein attributes

Sequence length	399 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.

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 – 399	399	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000296748
Regions
	Region	1 – 235	235	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	236 – 399	164	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	242	1	Divalent metal cation By similarity
	Metal binding	244	1	Divalent metal cation By similarity
	Metal binding	283	1	Divalent metal cation By similarity
	Site	15	1	Transition state stabilizer By similarity
	Site	24	1	Transition state stabilizer By similarity
	Site	160	1	Positions MEP for the nucleophilic attack By similarity
	Site	216	1	Positions MEP for the nucleophilic attack By similarity
	Site	275	1	Transition state stabilizer By similarity
	Site	374	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1MR76-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 5DA3E66FA1C0378C	FASTA	399	43,819
	10 20 30 40 50 60 METWALILAA GQGSRLLSTI GIAKQFFVWK GIPLYWQSVL QFMHCARIRG VVLVFPSEVK 70 80 90 100 110 120 DNEEKVVDRL AAQYDLRLPY IVISGGKLRQ DSVKNALNTL PKNCSHVLIH DAARPFISPK 130 140 150 160 170 180 LINNVIEVLE AGAVGVVPGI SVTDTIKQVI QGEVIVTRPR EQLIAVQTPQ GFHLKTIVEG 190 200 210 220 230 240 HNRATLEKWT VTDDASLLEL CGHTVQVING EIENRKISFP QDLLYMVEQP KTTVPIVGYG 250 260 270 280 290 300 YDVHKYVTED QINQPIRSMR LGGISIPNAP NVVAHSDGDV LLHALMDALL GCIGGGDIGL 310 320 330 340 350 360 HFPDSDKRYD GINSAILLDH VLTKVLESSI KIVHMDATIV AQLPKISQYR EAIRSNLSRL 370 380 390 LDLDLANVNI KATTEEGLGF TGECKGIKAI VIVTAIRIS

References

[1]

"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy." Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V. Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180252 Genomic DNA. Translation: CAJ54500.1.
RefSeq	YP_594822.1.
3D structure databases
SMR	Q1MR76. Positions 2-397.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1MR76.
Genome annotation databases
GeneID	4060193.
GenomeReviews	Gene locus LI0446 in contig AM180252_GR.
KEGG	lip:LI0446.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1211.
HOGENOM	HBG672839.
OMA	IVLIHDA.
PhylomeDB	Q1MR76.
Enzyme and pathway databases
BioCyc	LINT363253:LI0446-MONOMER.
Family and domain databases
HAMAP	MF_01520. IspDF. [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_LAWIP

Accession

Primary (citable) accession number: Q1MR76

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	May 30, 2006
Last modified:	February 9, 2010
This is version 25 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)