SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

C1B486

- C1B486_RHOOB

UniProt

C1B486 - C1B486_RHOOB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
1-deoxy-D-xylulose-5-phosphate synthase
Gene
dxs, ROP_68280
Organism
Rhodococcus opacus (strain B4)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotationSAAS annotations

Catalytic activityi

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2.UniRule annotationSAAS annotations

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotationSAAS annotations
Binds 1 thiamine pyrophosphate per subunit By similarity.UniRule annotationSAAS annotations

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891Thiamine pyrophosphate By similarityUniRule annotation
Metal bindingi161 – 1611Magnesium By similarityUniRule annotation
Metal bindingi191 – 1911Magnesium By similarityUniRule annotation
Binding sitei191 – 1911Thiamine pyrophosphate By similarityUniRule annotation
Binding sitei302 – 3021Thiamine pyrophosphate By similarityUniRule annotation
Binding sitei383 – 3831Thiamine pyrophosphate By similarityUniRule annotation

GO - Molecular functioni

  1. 1-deoxy-D-xylulose-5-phosphate synthase activity Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. thiamine pyrophosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 1-deoxy-D-xylulose 5-phosphate biosynthetic process Source: UniProtKB-UniPathway
  2. terpenoid biosynthetic process Source: UniProtKB-HAMAP
  3. thiamine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotationsImported

Keywords - Biological processi

Isoprene biosynthesisUniRule annotationSAAS annotations, Thiamine biosynthesisUniRule annotationSAAS annotations

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Thiamine pyrophosphateUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciROPA632772:GH0Q-6878-MONOMER.
UniPathwayiUPA00064; UER00091.

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose-5-phosphate synthaseUniRule annotation (EC:2.2.1.7UniRule annotation)
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase
Gene namesi
Name:dxsUniRule annotationImported
Ordered Locus Names:ROP_68280Imported
OrganismiRhodococcus opacus (strain B4)Imported
Taxonomic identifieri632772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000002212: Chromosome

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotationSAAS annotations

Protein-protein interaction databases

STRINGi632772.ROP_68280.

Structurei

3D structure databases

ProteinModelPortaliC1B486.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1323Thiamine pyrophosphate binding By similarityUniRule annotation
Regioni162 – 1632Thiamine pyrophosphate binding By similarityUniRule annotation

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1154.
HOGENOMiHOG000012986.
KOiK01662.
OMAiRINAGDP.
OrthoDBiEOG6BKJ6P.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
HAMAPiMF_00315. DXP_synth.
InterProiIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamiPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C1B486-1 [UniParc]FASTAAdd to Basket

« Hide

MAEARKAACI TEGAISLGVL ARIQTPDDLR QLNPAEMKQL AAEIREFLVQ    50
KVAATGGHLG PNLGVVELTL ALHRIFESPA DPIVFDTGHQ AYVHKILTGR 100
KDDFDSLRKQ GGLSGYPCRA ESDHDWVESS HASAALSYAD GLAKAFELTG 150
QARHVVAVVG DGALTGGMCW EALNNIAAGK DRSVVIVVND NGRSYAPTIG 200
GLADHLAALR LQPGYERILD SGRRMVKKLP WVGRTAYSVL HGMKAGLKDA 250
VAPQVMFTDL GIKYLGPVDG HDEAALESAL RRAKAFGGPV IVHAVTRKGM 300
GYAPAENHVA DQMHSTGVID PVTGKSAGSA SADWTSVFSA ELIDQASHRQ 350
DIVAITAAMA GPTGLAAFGE KYPDRMFDVG IAEQHAVTSA AGLALGGLHP 400
VVAVYSTFLN RAFDQLLMDV ALLKLPVTLV LDRAGITGSD GASHNGMWDM 450
SLLGIVPGMR VAAPRDTATL REELAEALAV DDGPTALRFP KGTVGDDVPA 500
VSRLDGVVDI LHAPSGRNDV LIVSVGAFAG LALAAAERLE QQGISATVVD 550
PRWVLPVPES LLKLAEDSTM VVTVEDSGLH GGVGSTVSAA LRAAGVDVPC 600
RDLGVPQRFL DHASRAQIHA ELGLTAQDVA RQITGWFAGL GNLRPGQQNG 650
VVADLDAQRA ENRGQ 665
Length:665
Mass (Da):69,831
Last modified:May 26, 2009 - v1
Checksum:iE0A94A32A2152E0E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011115 Genomic DNA. Translation: BAH55075.1.
RefSeqiYP_002784020.1. NC_012522.1.

Genome annotation databases

EnsemblBacteriaiBAH55075; BAH55075; ROP_68280.
GeneIDi7741621.
KEGGirop:ROP_68280.
PATRICi23231095. VBIRhoOpa21106_6912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011115 Genomic DNA. Translation: BAH55075.1 .
RefSeqi YP_002784020.1. NC_012522.1.

3D structure databases

ProteinModelPortali C1B486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 632772.ROP_68280.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH55075 ; BAH55075 ; ROP_68280 .
GeneIDi 7741621.
KEGGi rop:ROP_68280.
PATRICi 23231095. VBIRhoOpa21106_6912.

Phylogenomic databases

eggNOGi COG1154.
HOGENOMi HOG000012986.
KOi K01662.
OMAi RINAGDP.
OrthoDBi EOG6BKJ6P.

Enzyme and pathway databases

UniPathwayi UPA00064 ; UER00091 .
BioCyci ROPA632772:GH0Q-6878-MONOMER.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
HAMAPi MF_00315. DXP_synth.
InterProi IPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view ]
Pfami PF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00204. dxs. 1 hit.
PROSITEi PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: B4Imported.

Entry informationi

Entry nameiC1B486_RHOOB
AccessioniPrimary (citable) accession number: C1B486
Entry historyi
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi