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Reviewed, UniProtKB/Swiss-Prot Q0BE21 (DXR_BURCM)

Last modified June 16, 2009. Version 22. 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

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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: Bamb_2046
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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

Sequence similarities

Belongs to the DXR family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3983981-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020225

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

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Sequences

Sequence LengthMass (Da)Tools
Q0BE21-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 6948AC58295C840E

FASTA39842,199
        10         20         30         40         50         60 
MQKRLTLLGS TGSIGDSTLD VVARHPERFS VYALTAHRNG DKLVEQCLRF APEVAVVGDA 

        70         80         90        100        110        120 
NTAAHVEAKL RAAGSKTIVL YGPQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 

       130        140        150        160        170        180 
ILLANKESLV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDENEHGG ISKIILTASG 

       190        200        210        220        230        240 
GPFRTREPAT LADVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW IFGLAGDRID 

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

       310        320        330        340        350        360 
EKPDYTRFPC LALALKALEE GGIASAALNA ANEIAVEAFL ERRIGFMAIA ATVDAVLNAL 

       370        380        390 
PNRSPNGLDD VLAADAEARR LAAEIIAKAP APRVERTV

« Hide

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References

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

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Cross-references

Sequence databases

CP000440 Genomic DNA. Translation: ABI87602.1.
RefSeqYP_773936.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4311619.
GenomeReviewsGene locus Bamb_2046 in contig CP000440_GR.
KEGGbam:Bamb_2046.
NMPDRfig|339670.3.peg.6032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ0BE21. IHSMVEY.

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...

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Entry information

Entry nameDXR_BURCM
AccessionPrimary (citable) accession number: Q0BE21
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 22 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)

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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