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A5CT05 (A5CT05_CLAM3) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 38. 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:dxrA EMBL CAN02230.1
Synonyms:dxr HAMAP MF_00183
Ordered Locus Names:CMM_2160
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP] EMBL CAN02230.1
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Clavibacter

Protein attributes

Sequence length360 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 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

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
A5CT05 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 8E5CE3AA792ACCE0

FASTA36038,313
        10         20         30         40         50         60 
MRRVIILGST GSIGVQALEV VARHPELFEV VGLGAGSKRE ALAEQARVAG VEHTALGADE 

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

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

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

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

       310        320        330        340        350        360 
AANEQAVQAF HSGRAGFLDI VDTIRRVVDA HEPASGPLTR ESLAEAERWA RAEADRVLGV

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References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM711867 Genomic DNA. Translation: CAN02230.1.
RefSeqYP_001222905.1. NC_009480.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5CT05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5174690.
GenomeReviewsGene locus CMM_2160 in contig AM711867_GR.
KEGGcmi:CMM_2160.
PATRIC21455163. VBIClaMic82482_2288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
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 nameA5CT05_CLAM3
AccessionPrimary (citable) accession number: A5CT05
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 38 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