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Q28W25 (DXS2_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 synthase 2

EC=2.2.1.7
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase 2
Short name=DXP synthase 2
Short name=DXPS 2
Gene names
Name:dxs2
Ordered Locus Names:Jann_0170
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length636 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 MF_00315

Catalytic activity

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

Cofactor

Binds 1 thiamine pyrophosphate per subunit By similarity.

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 MF_00315

Subunit structure

Homodimer By similarity. HAMAP MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6366361-deoxy-D-xylulose-5-phosphate synthase 2 HAMAP MF_00315
PRO_0000256432

Sequences

Sequence LengthMass (Da)Tools
Q28W25 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 1A2377809ECD39F2

FASTA63666,801
        10         20         30         40         50         60 
MDRPHTPILD QVNYPSDLRR MSNADLAQCA DELRAEVISA VSETGGHLGS SLGVVELSVA 

        70         80         90        100        110        120 
IHAVFNTPYD KLVWDVGHQC YPHKVLTGRR DRIRTLRQKD GLSGFTKRSE SEYDPFGAAH 

       130        140        150        160        170        180 
SSTSISAALG FAAAQDLGEA TGDGIAVIGD GSISAGMAYE ALNNAGDLGK RLFVILNDNE 

       190        200        210        220        230        240 
MSIAPPVGAM SKYLTDLSAK SPLATLKDIA DGVASHLPEP IRQGAERARE LVTGHQPSAT 

       250        260        270        280        290        300 
LFEHLGFTYI GPVDGHDMEE LLTTLRAAKA RATGPVLIHA VTVKGKGYSP AELSDDCYHG 

       310        320        330        340        350        360 
VAKFDVATGQ QKKSAPNAPS YTSVFGQTLL NMAEADSRIV GVTAAMPGGT GISTLQKAKP 

       370        380        390        400        410        420 
NRVFDVGIAE QHAVTFSAGM AAGGLKPFCA IYSSFLQRGY DQIVHDVALQ SLPVRFMIDR 

       430        440        450        460        470        480 
AGLVGADGPT HAGAFDIGYL SALPNMTVMA CADEAELVHM MATAAAHNDG PIALRYPRGE 

       490        500        510        520        530        540 
GTGVALPDQG DVLEIGKGRV IQDGHDVAIL SFGAHLEEAK DAATALEARG LSVTVADARF 

       550        560        570        580        590        600 
AKPLDTTLID DLMTKHSALI TVEQGAVLGF GGLVLHHLAA TGQLDGRCAV RTLHLPDRFI 

       610        620        630 
DQASPAEMYA DAGLTADDIA QAALEAMGVE VLAARA 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD53087.1.
RefSeqYP_508112.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28W25.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28W25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3932607.
GenomeReviewsGene locus Jann_0170 in contig CP000264_GR.
KEGGjan:Jann_0170.
PATRIC22143936. VBIJanSp43325_0246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHBG571647.
OMAYPRGAFI.
PhylomeDBQ28W25.
ProtClustDBPRK12571.

Enzyme and pathway databases

BioCycJSP290400:JANN_0170-MONOMER.

Family and domain databases

HAMAPMF_00315. DXP_synth.
[Tree]
InterProIPR005477. Dxylulose-5-P_synthase.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK01662.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00204. Dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS2_JANSC
AccessionPrimary (citable) accession number: Q28W25
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families