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B0RDZ9 (B0RDZ9_CLAMS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP MF_00183
Short name=DXP reductoisomerase HAMAP MF_00183
EC=1.1.1.267 HAMAP MF_00183
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase HAMAP MF_00183
2-C-methyl-D-erythritol 4-phosphate synthase HAMAP MF_00183
Gene names
Name:dxr HAMAP MF_00183
Ordered Locus Names:CMS1853
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / JCM 9667) [Complete proteome] [HAMAP] EMBL CAQ01958.1
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Clavibacter

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 SAAS SAAS003821

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183 SAAS SAAS003821

Cofactor

Divalent cation By similarity. HAMAP MF_00183 SAAS SAAS003821

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183 SAAS SAAS003821

Sequence similarities

Belongs to the DXR family. HAMAP MF_00183

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential EMBL CAQ01958.1
Chain23 – 360338 Potential EMBL CAQ01958.1
PRO_5000307468

Regions

Nucleotide binding7 – 3630NADP By similarity HAMAP MF_00183

Sites

Metal binding1241Divalent metal cation By similarity HAMAP MF_00183
Metal binding1261Divalent metal cation By similarity HAMAP MF_00183
Metal binding1951Divalent metal cation By similarity HAMAP MF_00183
Binding site1011Substrate By similarity HAMAP MF_00183
Binding site1261Substrate By similarity HAMAP MF_00183
Binding site1501Substrate By similarity HAMAP MF_00183
Binding site1731Substrate By similarity HAMAP MF_00183
Binding site1951Substrate By similarity HAMAP MF_00183

Sequences

Sequence LengthMass (Da)Tools
B0RDZ9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5F6CDA7CEA2C2E20

FASTA36038,253
        10         20         30         40         50         60 
MRRVIVLGST GSIGVQALEV VARHPELFEV VGLGAGTQRE ALAEQARAAG VEHTALGADE 

        70         80         90        100        110        120 
AEQLIRSVDA DVVLNGITGS VGLGPTLAAL EEGRTLALAN KESLIVGGEL VRGLAAPGQL 

       130        140        150        160        170        180 
VPVDSEHSAI AQALRGGTAE EVRRLVVTAS GGPFRGRSRA ELEHVTPREA LAHPTWDMGL 

       190        200        210        220        230        240 
VITTNSSTLV NKGLEVIEAH LLFDVPYERI DVVVHPQSLV HSMVEFIDGS TLAQASPPDM 

       250        260        270        280        290        300 
RLPIALGLNW PHRMHDVGVP IDWTRAATWT FEPLDDEAFP AVLLAKQVGT AGSTYPAVYN 

       310        320        330        340        350        360 
AANEQAVQAF HAGRAGFLDI VDTIRRVVDA HEPASGPLTR ESLAEAERWT RAEADRVLGV

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References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed: 18192393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM849034 Genomic DNA. Translation: CAQ01958.1.
RefSeqYP_001710559.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RDZ9.
SMRB0RDZ9. Positions 2-359.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0RDZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6157586.
GenomeReviewsGene locus CMS1853 in contig AM849034_GR.
KEGGcms:CMS_1853.
PATRIC21460746. VBIClaMic4666_1919.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG430762.
OMAIHSMVEY.
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. 2 hits.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB0RDZ9_CLAMS
AccessionPrimary (citable) accession number: B0RDZ9
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info