Skip Header

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

Q9PKW8 (DXR_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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
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:TC_0343
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length379 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

Keywords
   Biological processIsoprene biosynthesis
   LigandMetal-binding
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processisoprenoid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity

Inferred from electronic annotation. Source: EC

NADPH binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3793791-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_0000163629

Regions

Nucleotide binding7 – 3630NADP By similarity

Sites

Metal binding1471Divalent metal cation By similarity
Metal binding1491Divalent metal cation By similarity
Metal binding2181Divalent metal cation By similarity
Binding site1221Substrate By similarity
Binding site1491Substrate By similarity
Binding site1731Substrate By similarity
Binding site1961Substrate By similarity
Binding site2181Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PKW8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8C897289B35087BC

FASTA37941,811
        10         20         30         40         50         60 
MKRLALIGST GSIGKQVLQV IREIPDAFVI ETLAAYGRNR ESLISQIREF SPRVVAVRDE 

        70         80         90        100        110        120 
TTYKELRKLF PHIEILSGEE GLIAVATAAS VDMTIVASSG IDALPAVMAS IQERKTIALA 

       130        140        150        160        170        180 
NKESLVAAGE LVTTLAKKNH VQILPIDSEH NALFQCLEGR DPSTIKKLIL TASGGPLRNK 

       190        200        210        220        230        240 
SKEELQKVTL QEVLKHPIWD MGPKITVDSS TLVNKGLEII EAFWLFGLQA VEIEAVIHPQ 

       250        260        270        280        290        300 
SLIHGMVEFC DGTILSVMNP PSMLFPIQHV LTFPDRYPSI ISGLNFLTNQ TLEFLPIDDE 

       310        320        330        340        350        360 
RFPSIRLAKD VLREGGSMGC FFNGANEALV QRFLSGEIAW YQIVSKLQTL MDKYVVRSCL 

       370 
SLEDILQVDS EARALASEC

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002160 Genomic DNA. Translation: AAF39204.1.
PIRG81712.
RefSeqNP_296721.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PKW8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1246386.
GenomeReviewsGene locus TC_0343 in contig AE002160_GR.
KEGGcmu:TC0343.
PATRIC20372094. VBIChlMur19118_0371.
TIGRTC_0343.

Phylogenomic databases

HOGENOMHBG430762.
OMAIHSMVEY.
PhylomeDBQ9PKW8.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycCMUR243161:TC_0343-MONOMER.

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_CHLMU
AccessionPrimary (citable) accession number: Q9PKW8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 73 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents