Skip Header

Contribute Send feedback
Read comments (?) or add your own

A2SB78 (DXR_BURM9) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BMA10229_A3261
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
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. HAMAP MF_00183

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. HAMAP MF_00183

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3983981-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020227

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
A2SB78 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 6500410CBCAA8463

FASTA39841,622
        10         20         30         40         50         60 
MQKRLTLLGS TGSIGDSTLD VVARHPERFA VHALTAHRNG EKLVAQCLRF APDVAVVGDA 

        70         80         90        100        110        120 
ETAARVEAQL RAAGSRTQVA YGKQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 

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

       190        200        210        220        230        240 
GPFRTREPAT LASVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW LFGLPSEHID 

       250        260        270        280        290        300 
VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVAQL DLAQIATLTF 

       310        320        330        340        350        360 
EKPDYARFPC LALAIDALEA GGVASAALNA ANEIAVDAFL SRRIRFTAIA QTVGAVLDGL 

       370        380        390 
SNRTPGGLDD VIEADAAARR AATAFIGKLP APGVERAA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000546 Genomic DNA. Translation: ABN03493.1.
RefSeqYP_001029197.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2SB78.
SMRA2SB78. Positions 2-392.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SB78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4792596.
GenomeReviewsGene locus BMA10229_A3261 in contig CP000546_GR.
KEGGbml:BMA10229_A3261.
PATRIC19137538. VBIBurMal46188_5454.
TIGRBMA10229_A3261.

Phylogenomic databases

HOGENOMHBG430762.
OMAIHSMVEY.
PhylomeDBA2SB78.
ProtClustDBPRK12464.

Family and domain databases

HAMAPMF_00183. DXP_reductoisom.
[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.
KOK00099.
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_BURM9
AccessionPrimary (citable) accession number: A2SB78
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families