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Q8KFI9 (DXS_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:CT0337
OrganismChlorobium tepidum
Taxonomic identifier1097 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

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 caution

The sequence AAM71583.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6356351-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315
PRO_0000189102

Sequences

Sequence LengthMass (Da)Tools
Q8KFI9 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: FC6B721D7CAD60EB

FASTA63568,883
        10         20         30         40         50         60 
MISQAYPLLS SIHSPADLKK LSLHELELVA AECRKKVIEL VSQNGGHFGS SLGVVELTVA 

        70         80         90        100        110        120 
LHYVYQSPTD RIIWDVGHQA YVHKILTGRL AQMETNRRYH GLAGFPKRSE SPHDAFGTGH 

       130        140        150        160        170        180 
ASTSISAAAG LAAARDLAGR KEKVVAIIGD GSLTGGMAFE AMNHLGDTKS DVLVILNDNQ 

       190        200        210        220        230        240 
MAISPSTGGL KNYLVNLTLN KTYNRLRKFV WDSLSLLHNE IGETAKTAVH RIEDGIKAAF 

       250        260        270        280        290        300 
TPGAYFEALG FRYFGPIDGH NMEQLIKALR EMRQLHHPKL LHVITTKGKG FKPAEENQPK 

       310        320        330        340        350        360 
WHASVGGFDI ETGKNVKAPG KPAKPKYQEV FGEALVELAL KDPTITAITA AMPSGTSLDL 

       370        380        390        400        410        420 
FQQAIPSRCF DVGIAEQHAV TFAAGLACGG FKPVFAVYST FLQRAYDQLI HDVALQNLHV 

       430        440        450        460        470        480 
VFAIDRAGLV GEDGPTHHGA FDLSYLNVVP NLTIMAPGDE QELRNMLYTA LYDIKGPVAI 

       490        500        510        520        530        540 
RYPRGSGSGA TLHKEFTPVP VGRGRILRDG KSVALLGIGT MSNRALETAA LLEAAGLDPL 

       550        560        570        580        590        600 
VCDMRFLKPL DTEIIDMAAS RCTHIVTIEE NSIIGGFGSN VVNYLHHAHP GIKCISFGLP 

       610        620        630 
DAFVTHGSMD ELYREVGLDA ESLSGKILEF YKDKP

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006470 Genomic DNA. Translation: AAM71583.1. Different initiation.
RefSeqNP_661241.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KFI9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1007999.
GenomeReviewsGene locus CT0337 in contig AE006470_GR.
KEGGcte:CT0337.
NMPDRfig|194439.1.peg.335.
PATRIC21398791. VBIChlTep116050_0327.
TIGRCT0337.

Phylogenomic databases

HOGENOMHBG571647.
OMAQYDISYM.
ProtClustDBPRK05444.

Enzyme and pathway databases

BioCycCTEP194439:CT_0337-MONOMER.

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.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_CHLTE
AccessionPrimary (citable) accession number: Q8KFI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: January 25, 2012
This is version 60 of the entry and version 2 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

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