A1W1K9 (ISPDF_CAMJJ) 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:	CJJ81176_1594

Organism

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]

Taxonomic identifier

354242 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	371 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: 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 – 371	371	Bifunctional enzyme IspD/IspF HAMAP MF_01520		PRO_0000296742
Regions
	Region	1 – 210	210	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	211 – 371	161	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	217	1	Divalent metal cation By similarity
	Metal binding	219	1	Divalent metal cation By similarity
	Metal binding	251	1	Divalent metal cation By similarity
	Site	16	1	Transition state stabilizer By similarity
	Site	23	1	Transition state stabilizer By similarity
	Site	139	1	Positions MEP for the nucleophilic attack By similarity
	Site	191	1	Positions MEP for the nucleophilic attack By similarity
	Site	243	1	Transition state stabilizer By similarity
	Site	342	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1W1K9 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 7CBAC2D4C942E5AE	FASTA	371	41,644
	10 20 30 40 50 60 MSEISLIMLA AGNSTRFNTK VKKQFLRLGN DPLWLYATKN LSSFYPFKKI VVTSSNISYM 70 80 90 100 110 120 KKFTKNYEFI EGGDTRAESL KKALELIDSE FVMVSDVARV LVSKNLFDRL IENLDKADCI 130 140 150 160 170 180 TPALKVADTT LFDNEALQRE KIKLIQTPQI SKTKLLKKAL DQNLEFTDDS TAIAAMGGKI 190 200 210 220 230 240 WFVEGEENAR KLTFKEDLKK LDLPTPSFEI FTGNGFDVHE FGENRPLLLA GVQIHPTMGL 250 260 270 280 290 300 KAHSDGDVLA HSLTDAILGA AGLGDIGELY PDTDMKFKNA NSMELLKQAY DKVREVGFEL 310 320 330 340 350 360 INIDICVMAQ SPKLKDFKQA MQSNIAHTLD LDEFRINVKA TTTEKLGFIG RKEGMAVLSS 370 VNLKYFDWTR L

References

[1]	Fouts D.E., Nelson K.E., Sebastian Y. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 81-176.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000538 Genomic DNA. Translation: EAQ72803.1.
RefSeq	YP_001001250.1. NC_008787.1.
3D structure databases
ProteinModelPortal	A1W1K9.
SMR	A1W1K9. Positions 2-370.
ModBase	Search...
Protein-protein interaction databases
STRING	A1W1K9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4683589.
GenomeReviews	Gene locus CJJ81176_1594 in contig CP000538_GR.
KEGG	cjj:CJJ81176_1594.
PATRIC	20053170. VBICamJej103413_1591.
TIGR	CJJ81176_1594.
Phylogenomic databases
eggNOG	COG1211.
HOGENOM	HBG672839.
OMA	IVLIHDA.
PhylomeDB	A1W1K9.
ProtClustDB	PRK09382.
Enzyme and pathway databases
BioCyc	CJEJ354242:CJJ81176_1594-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_CAMJJ

Accession

Primary (citable) accession number: A1W1K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program