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P64012 (DXR_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:Rv2870c, MT2938
ORF Names:MTCY274.01c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence caution

The sequence AAK47263.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4134131-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_0000163678

Regions

Nucleotide binding18 – 4730NADP By similarity

Sites

Metal binding1511Divalent metal cation By similarity
Metal binding1531Divalent metal cation By similarity
Metal binding2221Divalent metal cation By similarity
Binding site1281Substrate By similarity
Binding site1531Substrate By similarity
Binding site1771Substrate By similarity
Binding site2001Substrate By similarity
Binding site2221Substrate By similarity

Secondary structure

1 ...................................................................... 413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P64012 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 44E19577CE4D814F

FASTA41342,853
        10         20         30         40         50         60 
MTNSTDGRAD GRLRVVVLGS TGSIGTQALQ VIADNPDRFE VVGLAAGGAH LDTLLRQRAQ 

        70         80         90        100        110        120 
TGVTNIAVAD EHAAQRVGDI PYHGSDAATR LVEQTEADVV LNALVGALGL RPTLAALKTG 

       130        140        150        160        170        180 
ARLALANKES LVAGGSLVLR AARPGQIVPV DSEHSALAQC LRGGTPDEVA KLVLTASGGP 

       190        200        210        220        230        240 
FRGWSAADLE HVTPEQAGAH PTWSMGPMNT LNSASLVNKG LEVIETHLLF GIPYDRIDVV 

       250        260        270        280        290        300 
VHPQSIIHSM VTFIDGSTIA QASPPDMKLP ISLALGWPRR VSGAAAACDF HTASSWEFEP 

       310        320        330        340        350        360 
LDTDVFPAVE LARQAGVAGG CMTAVYNAAN EEAAAAFLAG RIGFPAIVGI IADVLHAADQ 

       370        380        390        400        410 
WAVEPATVDD VLDAQRWARE RAQRAVSGMA SVAIASTAKP GAAGRHASTL ERS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842581 Genomic DNA. Translation: CAA98375.2.
AE000516 Genomic DNA. Translation: AAK47263.1. Different initiation.
PIRA70923.
RefSeqNP_217386.2. NC_000962.2.
NP_337449.2. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C82X-ray1.90A/B1-413[»]
2JCVX-ray2.20A/B2-389[»]
2JCXX-ray2.10A/B2-389[»]
2JCYX-ray2.35A/B2-389[»]
2JCZX-ray2.05A/B2-389[»]
2JD0X-ray2.30A/B2-389[»]
2JD1X-ray2.00A/B2-389[»]
2JD2X-ray2.15A/B2-389[»]
2Y1CX-ray1.90A/B2-389[»]
2Y1DX-ray2.05A/B2-389[»]
2Y1EX-ray1.65A/B2-389[»]
2Y1FX-ray1.96A/B2-389[»]
2Y1GX-ray1.95A/B2-389[»]
3RASX-ray2.55A/B2-389[»]
ProteinModelPortalP64012.
SMRP64012. Positions 11-389.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000000352; EBMYCP00000000352; EBMYCG00000000352.
EBMYCT00000071333; EBMYCP00000069392; EBMYCG00000071328.
GeneID887800.
925338.
GenomeReviewsGene locus MT2938 in contig AE000516_GR.
Gene locus Rv2870c in contig AL123456_GR.
KEGGmtc:MT2938.
mtu:Rv2870c.
PATRIC18128232. VBIMycTub22151_3215.
TIGRMT2938.

Organism-specific databases

TubercuListRv2870c.

Phylogenomic databases

GeneTreeEBGT00050000016490.
HOGENOMHBG430762.
OMAIHSMVEY.
PhylomeDBP64012.
ProtClustDBPRK05447.

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_MYCTU
AccessionPrimary (citable) accession number: P64012
Secondary accession number(s): Q10798
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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