Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4SDG1 (DXS_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Cvib_0498
OrganismProsthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides (strain DSM 265)) [Complete proteome] [HAMAP]
Taxonomic identifier290318 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length635 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 – 6356351-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315
PRO_1000079097

Sequences

Sequence LengthMass (Da)Tools
A4SDG1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 9DCB70A4F6F634C1

FASTA63568,758
        10         20         30         40         50         60 
MADSRSLLDT INSPRDLKKL SIRQLETLAN ECRHELINLI SLNGGHFASS LGVTELSVAL 

        70         80         90        100        110        120 
HHVYNTEKDR IVWDVGHQAY IHKMLTGRRE RMNSNRKYGG ISGFPKIHES PHDAFGTGHA 

       130        140        150        160        170        180 
STSISAAAGI ASARDLKGGN EKVIAVIGDG SMTGGMAFEA MNHLGDLKND VLVILNDNQM 

       190        200        210        220        230        240 
AISPSTGGLK THMVNFTLNK TYNKARRLLW ESMSMMNNDL AERAKTSLRR LEDGMKAALT 

       250        260        270        280        290        300 
PGAFFEALGL RYFGPIDGHN MGQLVRALRE MQELPHPKLL HVITTKGKGF LPAEENQSDW 

       310        320        330        340        350        360 
HAHNGGFDTV TGITAKKEGP SATPKYQEVF GEALVEMALK DPAITAITAA MPTGTSLDLF 

       370        380        390        400        410        420 
QKAMPDRFYD VGIAEGHAVT FAAGQALEGL KPVCAIYSTF LQRALDQVIH DVALQNLPVV 

       430        440        450        460        470        480 
FAIDRAGLVG EDGPTHHGAF DLSYLHAVPG LTIMAPSDGQ ELRDMLHTAL YHIDGPVAIR 

       490        500        510        520        530        540 
YPRGSTGGEE MRKNFTALEP GKGRMLKEGT GPVILTLGTM AATALEAGRL LENEGISVEI 

       550        560        570        580        590        600 
ADMRFLKPLD TALIDRLSAS ATHIVTLEEN SIIGGFGSAV ADHLSEASKK TRLLRIGLPD 

       610        620        630 
AFVTHGSMTD LYRETGLDAP AVAEKIRLFY TGRES 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
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., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP36520.1.
RefSeqYP_001130022.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SDG1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SDG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4969543.
GenomeReviewsGene locus Cvib_0498 in contig CP000607_GR.
KEGGpvi:Cvib_0498.
PATRIC21395348. VBIChlPha132153_0526.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHBG571647.
OMADPILYHG.
PhylomeDBA4SDG1.
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.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[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. 1 hit.
PS00802. TRANSKETOLASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_PROVI
AccessionPrimary (citable) accession number: A4SDG1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 38 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