Reviewed, UniProtKB/Swiss-Prot Q0C0N0 (ISPDF_HYPNA)

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:	HNE_2014

Organism

Hyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]

Taxonomic identifier

228405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Hyphomonas

Protein attributes

Sequence length	378 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 – 378	378	Bifunctional enzyme ispD/ispF HAMAP MF_01520		PRO_0000292852
Regions
	Region	1 – 221	221	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
	Region	222 – 378	157	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520
Sites
	Metal binding	228	1	Divalent metal cation By similarity
	Metal binding	230	1	Divalent metal cation By similarity
	Metal binding	262	1	Divalent metal cation By similarity
	Site	16	1	Transition state stabilizer By similarity
	Site	23	1	Transition state stabilizer By similarity
	Site	148	1	Positions MEP for the nucleophilic attack By similarity
	Site	201	1	Positions MEP for the nucleophilic attack By similarity
	Site	254	1	Transition state stabilizer By similarity
	Site	353	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0C0N0-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: B5AB6F7A04775D5F	FASTA	378	39,494
	10 20 30 40 50 60 MTETVAIIVA GGRGQRAGAE RPKQWQMLLG KRVIDWSIAA FVDHPQISQV VIVAGDELGD 70 80 90 100 110 120 CSAEPKIIQA KPGNTRTQSV LSGLAAATIS EDATVVIHDA ARPGIDAATI SSLIARLQDP 130 140 150 160 170 180 SVSGAAPAMP VADALKTNSG QSWTNVDRTG LVRVQTPQAF RLGEIRAALS AAGPDLVDDL 190 200 210 220 230 240 TAIEAAGGRV EIVSGSARLT KITYPEDFDM LARLLSPTGA PRIGKGYDVH EFEAGDHVTL 250 260 270 280 290 300 CGVAIPHIAK LKGHSDADAA WHALTDAILG AVALGDIGDH FPPSDPQWKG ADSGLFLKEA 310 320 330 340 350 360 QRLAEAKGYV IANCDITVIC EAPKVKPHRE AMRARTAELL GLPLDAVSVK ATTTEGLGFT 370 GRREGIAAEA VALLMPKG

References

[1]

"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus." Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L. J. Bacteriol. 188:6841-6850(2006) [PubMed: 16980487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000158 Genomic DNA. Translation: ABI76497.1.
RefSeq	YP_760713.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4287822.
GenomeReviews	Gene locus HNE_2014 in contig CP000158_GR.
KEGG	hne:HNE_2014.
NMPDR	fig|228405.5.peg.1940.
TIGR	HNE_2014.
Phylogenomic databases
HOGENOM	Q0C0N0.
OMA	Q0C0N0. IVLIHDA.
Enzyme and pathway databases
BioCyc	HNEP81032:HNE_2014-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_HYPNA

Accession

Primary (citable) accession number: Q0C0N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 21 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)