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Reviewed, UniProtKB/Swiss-Prot A7H243 (DXR_CAMJD)

Last modified November 3, 2009. Version 16. 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:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase
      Short name=DXP reductoisomerase
    EC=1.1.1.267
Alternative name(s):
    1-deoxyxylulose-5-phosphate reductoisomerase
    2-C-methyl-D-erythritol 4-phosphate synthase
Gene names
Name: dxr
Ordered Locus Names: JJD26997_0364
OrganismCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]
Taxonomic identifier360109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity.

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183

Cofactor

Divalent cation By similarity.

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183

Sequence similarities

Belongs to the DXR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3563561-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020239

Regions

Nucleotide binding4 – 3027NADP By similarity

Sites

Metal binding1311Divalent metal cation By similarity
Metal binding1331Divalent metal cation By similarity
Metal binding2001Divalent metal cation By similarity
Binding site1121Substrate By similarity
Binding site1331Substrate By similarity
Binding site1551Substrate By similarity
Binding site1781Substrate By similarity
Binding site2001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H243-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: A7A55E93791DAE9A

FASTA35639,521
        10         20         30         40         50         60 
MILFGSTGSI GVNALKLAAL KNIPISALAC GDNIALLNEQ IARFKPQFVA IKDSKNKHLV 

        70         80         90        100        110        120 
KHDRVFIGQE GLEQILTECQ DRLLLNAIVG FAGLKSTLKA KELGKNIALA NKESLVVAGS 

       130        140        150        160        170        180 
FLKGAKFLPI DSEHVALKFL LEGKKNIAKL YITASGGAFY KYKIKDLNQV SVKDALKHPN 

       190        200        210        220        230        240 
WNMGAKITID SATMANKLFE IIEAYHLYDF KESDALIEPR SLVHAMCEFK NGASTAYFSK 

       250        260        270        280        290        300 
ADMKLAISDA IFEKQDTPIL EAVDFSKMPA LKFHKISTKK YPIFKLKNAF LKEPNLGVII 

       310        320        330        340        350 
NAANEVGVYN FLENKSGFLD IAQCIFKALD HFGAPKISSI EEVFEYDFKT REYLRS 

« Hide

References

[1]"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000768 Genomic DNA. Translation: ABS43260.1.
RefSeqYP_001397573.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7H243.

Genome annotation databases

GeneID5390301.
GenomeReviewsGene locus JJD26997_0364 in contig CP000768_GR.
KEGGcjd:JJD26997_0364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIHSMVEY.

Family and domain databases

HAMAPMF_00183.
[Tree]
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
[Graphical view]
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDXR_CAMJD
AccessionPrimary (citable) accession number: A7H243
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 16 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