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Reviewed, UniProtKB/Swiss-Prot A0K8D7 (DXR_BURCH)

Last modified November 3, 2009. Version 24. 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: Bcen2424_2013
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length398 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 – 3983981-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020224

Regions

Nucleotide binding8 – 3730NADP By similarity

Sites

Metal binding1511Divalent metal cation By similarity
Metal binding1531Divalent metal cation By similarity
Metal binding2241Divalent metal cation By similarity
Binding site1261Substrate By similarity
Binding site1531Substrate By similarity
Binding site1791Substrate By similarity
Binding site2021Substrate By similarity
Binding site2241Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0K8D7-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: F8E11B68AA2256C5

FASTA39841,924
        10         20         30         40         50         60 
MQKRLTLLGS TGSIGDSTLD VVARHPERFS VYALTAHRNG DKLVEQCLRF APEVAVVGDA 

        70         80         90        100        110        120 
ATAAHVDAKL RAAGSKTVVL HGPQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 

       130        140        150        160        170        180 
ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG ISKIILTASG 

       190        200        210        220        230        240 
GPFRTREPAT LVDVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW IFGLPGDRID 

       250        260        270        280        290        300 
VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVDQL DLAQIAQLSF 

       310        320        330        340        350        360 
EKPDYARFPC LALALKALEE GGIASAALNA ANEVAVEAFL ERRIGFMAIA ATVDAVLNTL 

       370        380        390 
PNRAPDGLDD VLAADAEARR LAAAIIAKAP APRVERTV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000458 Genomic DNA. Translation: ABK08764.1.
RefSeqYP_835657.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0K8D7.

Genome annotation databases

GeneID4448969.
GenomeReviewsGene locus Bcen2424_2013 in contig CP000458_GR.
KEGGbch:Bcen2424_2013.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMA0K8D7.
OMAIHSMVEY.

Family and domain databases

HAMAPMF_00183.
[Tree]
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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_BURCH
AccessionPrimary (citable) accession number: A0K8D7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 24 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