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C1B486 (C1B486_RHOOB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315

EC=2.2.1.7 HAMAP-Rule MF_00315
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase HAMAP-Rule MF_00315
Gene names
Name:dxs HAMAP-Rule MF_00315 EMBL BAH55075.1
Ordered Locus Names:ROP_68280 EMBL BAH55075.1
OrganismRhodococcus opacus (strain B4) [Complete proteome] [HAMAP] EMBL BAH55075.1
Taxonomic identifier632772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP) By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Catalytic activity

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. HAMAP-Rule MF_00315 SAAS SAAS005477

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Binds 1 thiamine pyrophosphate per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Pathway

Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1. HAMAP-Rule MF_00315 SAAS SAAS005477

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Sequence similarities

Belongs to the transketolase family. DXPS subfamily. HAMAP-Rule MF_00315

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region130 – 1323Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315
Region162 – 1632Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Sites

Metal binding1611Magnesium By similarity HAMAP-Rule MF_00315
Metal binding1911Magnesium By similarity HAMAP-Rule MF_00315
Binding site891Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site1911Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site3021Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site3831Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Sequences

Sequence LengthMass (Da)Tools
C1B486 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: E0A94A32A2152E0E

FASTA66569,831
        10         20         30         40         50         60 
MAEARKAACI TEGAISLGVL ARIQTPDDLR QLNPAEMKQL AAEIREFLVQ KVAATGGHLG 

        70         80         90        100        110        120 
PNLGVVELTL ALHRIFESPA DPIVFDTGHQ AYVHKILTGR KDDFDSLRKQ GGLSGYPCRA 

       130        140        150        160        170        180 
ESDHDWVESS HASAALSYAD GLAKAFELTG QARHVVAVVG DGALTGGMCW EALNNIAAGK 

       190        200        210        220        230        240 
DRSVVIVVND NGRSYAPTIG GLADHLAALR LQPGYERILD SGRRMVKKLP WVGRTAYSVL 

       250        260        270        280        290        300 
HGMKAGLKDA VAPQVMFTDL GIKYLGPVDG HDEAALESAL RRAKAFGGPV IVHAVTRKGM 

       310        320        330        340        350        360 
GYAPAENHVA DQMHSTGVID PVTGKSAGSA SADWTSVFSA ELIDQASHRQ DIVAITAAMA 

       370        380        390        400        410        420 
GPTGLAAFGE KYPDRMFDVG IAEQHAVTSA AGLALGGLHP VVAVYSTFLN RAFDQLLMDV 

       430        440        450        460        470        480 
ALLKLPVTLV LDRAGITGSD GASHNGMWDM SLLGIVPGMR VAAPRDTATL REELAEALAV 

       490        500        510        520        530        540 
DDGPTALRFP KGTVGDDVPA VSRLDGVVDI LHAPSGRNDV LIVSVGAFAG LALAAAERLE 

       550        560        570        580        590        600 
QQGISATVVD PRWVLPVPES LLKLAEDSTM VVTVEDSGLH GGVGSTVSAA LRAAGVDVPC 

       610        620        630        640        650        660 
RDLGVPQRFL DHASRAQIHA ELGLTAQDVA RQITGWFAGL GNLRPGQQNG VVADLDAQRA 


ENRGQ 

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References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4 EMBL BAH55075.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011115 Genomic DNA. Translation: BAH55075.1.
RefSeqYP_002784020.1. NC_012522.1.

3D structure databases

ProteinModelPortalC1B486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING632772.ROP_68280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH55075; BAH55075; ROP_68280.
GeneID7741621.
KEGGrop:ROP_68280.
PATRIC23231095. VBIRhoOpa21106_6912.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHOG000012986.
KOK01662.
OMAAINHAGH.
OrthoDBEOG6BKJ6P.
ProtClustDBPRK05444.

Enzyme and pathway databases

BioCycROPA632772:GH0Q-6878-MONOMER.
UniPathwayUPA00064; UER00091.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
HAMAPMF_00315. DXP_synth.
InterProIPR005477. Dxylulose-5-P_synthase.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00204. dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1B486_RHOOB
AccessionPrimary (citable) accession number: C1B486
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)