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Protein

1-deoxy-D-xylulose-5-phosphate synthase

Gene

dxs

Organism
Shewanella baltica (strain OS195)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

Pathwayi: 1-deoxy-D-xylulose 5-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 1-deoxy-D-xylulose-5-phosphate synthase (dxs)
This subpathway is part of the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate, the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80Thiamine pyrophosphateUniRule annotation1
Metal bindingi152MagnesiumUniRule annotation1
Metal bindingi181MagnesiumUniRule annotation1
Binding sitei181Thiamine pyrophosphateUniRule annotation1
Binding sitei288Thiamine pyrophosphateUniRule annotation1
Binding sitei370Thiamine pyrophosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Isoprene biosynthesis, Thiamine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

UniPathwayiUPA00064; UER00091.

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose-5-phosphate synthaseUniRule annotation (EC:2.2.1.7UniRule annotation)
Alternative name(s):
1-deoxyxylulose-5-phosphate synthaseUniRule annotation
Short name:
DXP synthaseUniRule annotation
Short name:
DXPSUniRule annotation
Gene namesi
Name:dxsUniRule annotation
Ordered Locus Names:Sbal195_1382
OrganismiShewanella baltica (strain OS195)
Taxonomic identifieri399599 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000770 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000791021 – 6221-deoxy-D-xylulose-5-phosphate synthaseAdd BLAST622

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA9KTL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni121 – 123Thiamine pyrophosphate bindingUniRule annotation3
Regioni153 – 154Thiamine pyrophosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.
OrthoDBiPOG091H015K.

Family and domain databases

CDDicd02007. TPP_DXS. 1 hit.
Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth. 1 hit.
InterProiIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9KTL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDISQFPV LAQANTPNEL RQLPQALLPQ VADELREFLL KSVGISSGHF
60 70 80 90 100
ASGLGTVELT VALHYVYNTP FDRLIWDVGH QAYPHKILTG RRDKMHTIRQ
110 120 130 140 150
KDGLHPFPWR EESEYDTFSV GHSGTSISAA LAMAIAAEKE QAGRKVVAVI
160 170 180 190 200
GDGAMTGGMV FEAMNHAGDL HNDMLVVLND NEMSISENVG ALNNHLAQLM
210 220 230 240 250
SGRFYTTLRE GGKKVLKGMP VIKEMAKRTE EHLKGMVVPG TLFEELGFNY
260 270 280 290 300
IGPIDGHDVD ALVETMRNMR NLKGPQVLHI MTKKGRGYEP AEKDPIGWHA
310 320 330 340 350
VPKFDPSLFK KPATKPGLPT FSQVFGKWLC DIAEQDEKVL AITPAMREGS
360 370 380 390 400
GMVEFSQRFP KQYFDAAIAE QHAVTLAAGF ACEGFKPVVA IYSTFLQRAY
410 420 430 440 450
DQLIHDVALQ QLPVLFAIDR GGIVGADGPT HQGAFDLSFM RCIPNMVIMA
460 470 480 490 500
PSDENECRQM LYTGYCYDAG PSAVRYPRGS ATGAMQVEAM TALPIGKGVI
510 520 530 540 550
KRVGKRIAIL NFGTLLASAL TAAESLDATV VDMRFVKPLD VDLVKEMAQT
560 570 580 590 600
HEVLVTVEEN AIMGGAGAGV LEQLQKLRMP KAVLQIGLPD EFIKHGSPEE
610 620
VTHDLQLDAE GILAQINAYL AQ
Length:622
Mass (Da):68,019
Last modified:February 5, 2008 - v1
Checksum:i9F5284863D5B00E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX48556.1.
RefSeqiWP_006085152.1. NC_009997.1.

Genome annotation databases

EnsemblBacteriaiABX48556; ABX48556; Sbal195_1382.
GeneIDi11771638.
KEGGisbn:Sbal195_1382.
PATRICi23468842. VBISheBal33754_1438.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX48556.1.
RefSeqiWP_006085152.1. NC_009997.1.

3D structure databases

ProteinModelPortaliA9KTL5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX48556; ABX48556; Sbal195_1382.
GeneIDi11771638.
KEGGisbn:Sbal195_1382.
PATRICi23468842. VBISheBal33754_1438.

Phylogenomic databases

HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.
OrthoDBiPOG091H015K.

Enzyme and pathway databases

UniPathwayiUPA00064; UER00091.

Family and domain databases

CDDicd02007. TPP_DXS. 1 hit.
Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth. 1 hit.
InterProiIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDXS_SHEB9
AccessioniPrimary (citable) accession number: A9KTL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: November 2, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.