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Q48F65 (DXR_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:PSPPH_3834
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length396 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-Rule MF_00183

Catalytic activity

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

Cofactor

Divalent cation By similarity. HAMAP-Rule MF_00183

Pathway

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

Sequence similarities

Belongs to the DXR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3963961-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP-Rule MF_00183
PRO_0000163699

Regions

Nucleotide binding10 – 3930NADP By similarity

Sites

Metal binding1531Divalent metal cation By similarity
Metal binding1551Divalent metal cation By similarity
Metal binding2291Divalent metal cation By similarity
Binding site1281Substrate By similarity
Binding site1551Substrate By similarity
Binding site1841Substrate By similarity
Binding site2071Substrate By similarity
Binding site2291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48F65 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B62688A0E2E36A97

FASTA39642,342
        10         20         30         40         50         60 
MSGPQHITIL GATGSIGLST LDVVARHPSR YQVFALTGFS RLDELLALCV RHTPQYAVVP 

        70         80         90        100        110        120 
DQFVARKLQD DLAAAVLDTR VLVGEGGLCE VAAHPRVDAV MAAIVGAAGL RPTLAAVEAG 

       130        140        150        160        170        180 
KKVLLANKEA LVMSGDLFMQ AVRQSGAVLL PIDSEHNAIF QCLPGDFARG LGAVGVRRIM 

       190        200        210        220        230        240 
LTASGGPFRE TPLEQLQNVT PEQACAHPVW SMGRKISVDS ATMMNKGLEL IEACWLFDAR 

       250        260        270        280        290        300 
PDQVEVVIHP QSVIHSLVDY VDGSVLAQLG NPDMRTPIAN ALAWPARVDS GVAPLDLFRI 

       310        320        330        340        350        360 
GQLDFQKPDE ERFPCLRLAR HAAEAGGSAP AMLNAANEVA VAAFLDGRIR YLEIAGIIEE 

       370        380        390 
VLNHEPVTAV EGLDAVFAAD AKARLLAGQW LERNAR 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ37105.1.
RefSeqYP_275972.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48F65.
SMRQ48F65. Positions 5-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_3834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ37105; AAZ37105; PSPPH_3834.
GeneID3559744.
KEGGpsp:PSPPH_3834.
PATRIC19977109. VBIPseSyr78478_4015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
HOGENOMHOG000007221.
KOK00099.
OMAAHPNWVM.
OrthoDBEOG6R2H04.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-3837-MONOMER.
UniPathwayUPA00056; UER00092.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00183. DXP_reductoisom.
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR30525. PTHR30525. 1 hit.
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMSSF69055. SSF69055. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDXR_PSE14
AccessionPrimary (citable) accession number: Q48F65
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways