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Reviewed, UniProtKB/Swiss-Prot Q9ZM19 (ISPDF_HELPJ)

Last modified November 3, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: jhp_0404
OrganismHelicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000075670

Regions

Region1 – 2502502-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region251 – 4091592-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2571Divalent metal cation By similarity
Metal binding2591Divalent metal cation By similarity
Metal binding2911Divalent metal cation By similarity
Site511Transition state stabilizer By similarity
Site581Transition state stabilizer By similarity
Site1781Positions MEP for the nucleophilic attack By similarity
Site2301Positions MEP for the nucleophilic attack By similarity
Site2831Transition state stabilizer By similarity
Site3821Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZM19-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 636B714E255DCF80

FASTA40945,706
        10         20         30         40         50         60 
MSLIRVNGEA FKLSLESLEE DPFETKETLE TLETLIKQTS VVLLAAGESK RFSRAIKKQW 

        70         80         90        100        110        120 
LRSHHTPLWL SVYESFKEAL DFKEVILVVS ELDYVYIQRH YPKIKLVKGG ASRQESVRNA 

       130        140        150        160        170        180 
LKVIDSTYTI TSDVARGLAN MEALKSLFLT LQQTSHYCIA PYLPCYDTAI YYNEALDREA 

       190        200        210        220        230        240 
IKLIQTPQLS HTKTLQSALN QGGFKDESSA ILQAFPNSVS YIEGSKDLHK LTTSGDLKFF 

       250        260        270        280        290        300 
TPFFNPAKDT FIGMGFDTHA FIKDKPMVLG GVVLDCEFGL KAHSDGDALL HAVIDAILGA 

       310        320        330        340        350        360 
IKGGDIGEWF PDNDPKYKNA SSKELLKIVL DFSQSIGFEL LEMGATIFSE IPKITPYKPA 

       370        380        390        400 
ILENLSQLLG LEKSQISLKA TTMEKMGFIG KQEGLLVQAH VSMRYKQKL 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE001439 Genomic DNA. Translation: AAD05981.1.
PIRG71936.
RefSeqNP_223123.1.

3D structure databases

HSSPHSSP built from PDB template 1GX1 based on UniProtKB P36663.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ZM19.

Genome annotation databases

GeneID889224.
GenomeReviewsGene locus jhp_0404 in contig AE001439_GR.
KEGGhpj:jhp0404.
NMPDRfig|85963.1.peg.401.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9ZM19.
OMAGGDIGEW.

Enzyme and pathway databases

BioCycHPYL85963:JHP0404-MON.
BRENDA2.7.7.60. 295085.
4.6.1.12. 295085.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_HELPJ
AccessionPrimary (citable) accession number: Q9ZM19
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents