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B2RMK4 (DXS_PORG3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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

EC=2.2.1.7
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase
Short name=DXP synthase
Short name=DXPS
Gene names
Name:dxs
Ordered Locus Names:PGN_2081
OrganismPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257) [Complete proteome] [HAMAP]
Taxonomic identifier431947 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length634 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 – 6346341-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315
PRO_1000115755

Sequences

Sequence LengthMass (Da)Tools
B2RMK4 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: F18BEC685FB372C1

FASTA63470,303
        10         20         30         40         50         60 
MMEVRPTTLI DHINSPADLR ALKPEQLPQV CRELRRYILE VLSVTPGHLG SSLGAVDFTV 

        70         80         90        100        110        120 
ALHYVFDTPY DRIVWDVGHQ AYSHKILTGR REDFRHLRQW GGISGFPSPK ESEYDTFPAG 

       130        140        150        160        170        180 
HASNSISAAL GMAVASAAKD EKRKVIAVIG DGSMTGGMAF EGLNNASSFP NNLLIILNDN 

       190        200        210        220        230        240 
NMSIDRNVGG LNRYMVDILT SKTYNTIRYD LYKGLRKINL ISETNRKNLL RFNNSFKALL 

       250        260        270        280        290        300 
ARESNLFEGF SIRYFGPVDG NNVLRLVEVL NQIKDMAGPK ILHLRTIKGK GYSPAEKQAT 

       310        320        330        340        350        360 
IWHAPGEFDI KSGERKKGEN KPEPPKFQDV FGHTLVELAD RDERIVGVTP AMPTGCSMTF 

       370        380        390        400        410        420 
LMKKYPNRAY DVGIAEGHAV TFSAGLAKEG LIPFCNIYSS FIQRGYDQVI HDVALSGSHV 

       430        440        450        460        470        480 
VICLDRAGLV GEDGATHHGV FDMAFLRCVP DIVVASPLNE HELRNLMLTA YKGYDGPMVI 

       490        500        510        520        530        540 
RYPRGKGVLT DWRNTPRLVE IARGRCLTEG EAIAFLSIGP IGNMVQKVVE RLAEKGVSAA 

       550        560        570        580        590        600 
HYDMVFLKPL DEEMLHGIAK KFDTIISVED GCIQGGFGSA VMEFMADHDY HPRIRRVGVP 

       610        620        630 
DRFIGQGSVP EQYADCGMDA DSLLHLTEEL LLHP 

« Hide

References

[1]"Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis."
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., Nakayama K.
DNA Res. 15:215-225(2008) [PubMed: 18524787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33277 / DSM 20709 / JCM 12257.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009380 Genomic DNA. Translation: BAG34599.1.
RefSeqYP_001930196.1. NC_010729.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2RMK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6329559.
GenomeReviewsGene locus PGN_2081 in contig AP009380_GR.
KEGGpgn:PGN_2081.
PATRIC22977131. VBIPorGin26334_2045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG571647.
OMAEAMNAHA.
ProtClustDBPRK05444.

Family and domain databases

HAMAPMF_00315. DXP_synth.
[Tree]
InterProIPR005477. Dxylulose-5-P_synthase.
IPR011766. TPP_enzyme-bd_C.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK01662.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF02779. 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. False negative.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_PORG3
AccessionPrimary (citable) accession number: B2RMK4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 28 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