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Q9JW13 (DXS_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. 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:NMA0589
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length637 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

Catalytic activity

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

Cofactor

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

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-Rule MF_00315

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6376371-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315
PRO_0000189133

Regions

Region117 – 1193Thiamine pyrophosphate binding By similarity
Region149 – 1502Thiamine pyrophosphate binding By similarity

Sites

Metal binding1481Magnesium By similarity
Metal binding1771Magnesium By similarity
Binding site761Thiamine pyrophosphate By similarity
Binding site1771Thiamine pyrophosphate By similarity
Binding site2941Thiamine pyrophosphate By similarity
Binding site3811Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JW13 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3B2BBD01AAD182F5

FASTA63768,720
        10         20         30         40         50         60 
MNPSPLLDLI DSPQDLRRLD KKQLPRLAGE LRTFLLESVG QTGGHFASNL GAVELTVALH 

        70         80         90        100        110        120 
YVYNTPEDKL VWDVGHQSYP HKILTGRKNQ MHTMRQYGGL AGFPKRCESE YDAFGVGHSS 

       130        140        150        160        170        180 
TSIGAALGMA AADKQLGSDR RSVAIIGDGA MTAGQAFEAL NCAGDMDVDL LVVLNDNEMS 

       190        200        210        220        230        240 
ISPNVGALPK YLASNVVRDM HGLLSTVKAQ TGKVLDKIPG AMEFAQKVEH KIKTLAEEAE 

       250        260        270        280        290        300 
HAKQSLSLFE NFGFRYTGPV DGHNVENLVD VLEDLRGRKG PQLLHVITKK GNGYKLAEND 

       310        320        330        340        350        360 
PVKYHAVANL PKESAAQMPS EKEPKPAAKP TYTQVFGKWL CDRAAADSRL VAITPAMREG 

       370        380        390        400        410        420 
SGLVEFEQRF PDRYFDVGIA EQHAVTFAGG LACEGMKPVV AIYSTFLQRA YDQLVHDIAL 

       430        440        450        460        470        480 
QNLPVLFAVD RAGIVGADGP THAGLYDLSF LRCIPNMIVA APSDENECRL LLSTCYQADA 

       490        500        510        520        530        540 
PAAVRYPRGT GTGVPVSDGM ETVEIGKGII RREGEKTAFI AFGSMVAPAL AVAGKLNATV 

       550        560        570        580        590        600 
ADMRFVKPID EELIVRLARS HDRIVTLEEN AEQGGAGSAV LEVLAKHGIC KPVLLLGVAD 

       610        620        630 
TVTGHGDPKK LLDDLGLSAE AVERRVRAWL SDRDAAN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM07859.1.
PIRB81978.
RefSeqYP_002342065.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JW13.
SMRQ9JW13. Positions 1-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA0589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM07859; CAM07859; NMA0589.
GeneID906582.
KEGGnma:NMA0589.
PATRIC20361956. VBINeiMen132687_0693.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHOG000012988.
KOK01662.
OMAAATCETF.
OrthoDBEOG6BKJ6P.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-555-MONOMER.
UniPathwayUPA00064; UER00091.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPMF_00315. DXP_synth.
InterProIPR005477. 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]
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]
SUPFAMSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00204. dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_NEIMA
AccessionPrimary (citable) accession number: Q9JW13
Secondary accession number(s): A1IQ33
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways