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Reviewed, UniProtKB/Swiss-Prot Q3MDL2 (DXR_ANAVT)

Last modified February 9, 2010. Version 31. 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

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: Ava_1300
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3983981-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020213

Regions

Nucleotide binding7 – 3630NADP By similarity

Sites

Metal binding1501Divalent metal cation By similarity
Metal binding1521Divalent metal cation By similarity
Metal binding2211Divalent metal cation By similarity
Binding site1251Substrate By similarity
Binding site1521Substrate By similarity
Binding site1761Substrate By similarity
Binding site1991Substrate By similarity
Binding site2211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MDL2-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 4AA74AB2321D3130

FASTA39843,055
        10         20         30         40         50         60 
MKSITLVGST GSIGTQTLDI VSQYPDQFRI VGLAAGSNVE MLAEQIRQFR PQIAAISAAE 

        70         80         90        100        110        120 
KLPALQAAIK DLDPQPILLG GEAGVIEVAR YGDAETVVTG IVGCAGLLPT IAAIEAGKDI 

       130        140        150        160        170        180 
ALANKETLIA GGPVVLPLVE KHGVKLLPAD SEHSAIFQCL QGVPKGGLRK ILLTASGGAF 

       190        200        210        220        230        240 
RDWDVERLAE VTVADALKHP NWSMGRKITV DSATLMNKGL EVIEAHFLFG LDYQDIEIVI 

       250        260        270        280        290        300 
HPQSIIHSLI ELQDTSVLAQ LGWPDMRLPL LYALSWPERI YTDWEPLNLV KAGNLTFREP 

       310        320        330        340        350        360 
DHQKYPCMQL AYAAGRAGGS MPAVLNAANE QVVALFLDEK IKFLDIPRCI ELVCDRHQND 

       370        380        390 
NCANPSLDDI LAADQWARQE VLTATKNLAS QPQIISVN 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA20924.1.
RefSeqYP_321819.1.

3D structure databases

SMRQ3MDL2. Positions 2-391.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MDL2.

Genome annotation databases

GeneID3683043.
GenomeReviewsGene locus Ava_1300 in contig CP000117_GR.
KEGGava:Ava_1300.
NMPDRfig|240292.3.peg.2145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
HOGENOMHBG430762.
OMAIHSMVEY.
PhylomeDBQ3MDL2.

Enzyme and pathway databases

BioCycAVAR240292:AVA_1300-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]
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_ANAVT
AccessionPrimary (citable) accession number: Q3MDL2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: February 9, 2010
This is version 31 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)

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