UniProtKB - P54523 (DXS_BACSU)
Protein
1-deoxy-D-xylulose-5-phosphate synthase
Gene
dxs
Organism
Bacillus subtilis (strain 168)
Status
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
- D-glyceraldehyde 3-phosphate + H+ + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2UniRule annotationEC:2.2.1.7UniRule 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
: 1-deoxy-D-xylulose 5-phosphate biosynthesis Pathwayi
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 annotationProteins known to be involved in this subpathway in this organism are:
- 1-deoxy-D-xylulose-5-phosphate synthase (dxs), 1-deoxy-D-xylulose-5-phosphate synthase (dxs)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 72 | Thiamine pyrophosphateUniRule annotation | 1 | |
Metal bindingi | 144 | MagnesiumUniRule annotation | 1 | |
Metal bindingi | 173 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 173 | Thiamine pyrophosphateUniRule annotation | 1 | |
Binding sitei | 284 | Thiamine pyrophosphateUniRule annotation | 1 | |
Binding sitei | 367 | Thiamine pyrophosphateUniRule annotation | 1 |
GO - Molecular functioni
- 1-deoxy-D-xylulose-5-phosphate synthase activity Source: GO_Central
- magnesium ion binding Source: UniProtKB-UniRule
- thiamine pyrophosphate binding Source: UniProtKB-UniRule
- transferase activity, transferring aldehyde or ketonic groups Source: GO_Central
GO - Biological processi
- 1-deoxy-D-xylulose 5-phosphate biosynthetic process Source: UniProtKB-UniPathway
- isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: GO_Central
- terpenoid biosynthetic process Source: UniProtKB-UniRule
- thiamine biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Transferase |
Biological process | Isoprene biosynthesis, Thiamine biosynthesis |
Ligand | Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | BSUB:BSU24270-MONOMER MetaCyc:BSU24270-MONOMER |
UniPathwayi | UPA00064;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 Synonyms:yqiE Ordered Locus Names:BSU24270 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000189086 | 1 – 633 | 1-deoxy-D-xylulose-5-phosphate synthaseAdd BLAST | 633 |
Proteomic databases
PaxDbi | P54523 |
PRIDEi | P54523 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationProtein-protein interaction databases
STRINGi | 224308.BSU24270 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 113 – 115 | Thiamine pyrophosphate bindingUniRule annotation | 3 | |
Regioni | 145 – 146 | Thiamine pyrophosphate bindingUniRule annotation | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1154, Bacteria |
InParanoidi | P54523 |
OMAi | QVGYHAQ |
PhylomeDBi | P54523 |
Family and domain databases
CDDi | cd02007, TPP_DXS, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
HAMAPi | MF_00315, DXP_synth, 1 hit |
InterProi | View protein in InterPro IPR005477, Dxylulose-5-P_synthase IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR005474, Transketolase_N |
PANTHERi | PTHR43322, PTHR43322, 1 hit |
Pfami | View protein in Pfam PF13292, DXP_synthase_N, 1 hit PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00204, dxs, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P54523-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDLLSIQDPS FLKNMSIDEL EKLSDEIRQF LITSLSASGG HIGPNLGVVE
60 70 80 90 100
LTVALHKEFN SPKDKFLWDV GHQSYVHKLL TGRGKEFATL RQYKGLCGFP
110 120 130 140 150
KRSESEHDVW ETGHSSTSLS GAMGMAAARD IKGTDEYIIP IIGDGALTGG
160 170 180 190 200
MALEALNHIG DEKKDMIVIL NDNEMSIAPN VGAIHSMLGR LRTAGKYQWV
210 220 230 240 250
KDELEYLFKK IPAVGGKLAA TAERVKDSLK YMLVSGMFFE ELGFTYLGPV
260 270 280 290 300
DGHSYHELIE NLQYAKKTKG PVLLHVITKK GKGYKPAETD TIGTWHGTGP
310 320 330 340 350
YKINTGDFVK PKAAAPSWSG LVSGTVQRMA REDGRIVAIT PAMPVGSKLE
360 370 380 390 400
GFAKEFPDRM FDVGIAEQHA ATMAAAMAMQ GMKPFLAIYS TFLQRAYDQV
410 420 430 440 450
VHDICRQNAN VFIGIDRAGL VGADGETHQG VFDIAFMRHI PNMVLMMPKD
460 470 480 490 500
ENEGQHMVHT ALSYDEGPIA MRFPRGNGLG VKMDEQLKTI PIGTWEVLRP
510 520 530 540 550
GNDAVILTFG TTIEMAIEAA EELQKEGLSV RVVNARFIKP IDEKMMKSIL
560 570 580 590 600
KEGLPILTIE EAVLEGGFGS SILEFAHDQG EYHTPIDRMG IPDRFIEHGS
610 620 630
VTALLEEIGL TKQQVANRIR LLMPPKTHKG IGS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D84432 Genomic DNA Translation: BAA12576.1 AL009126 Genomic DNA Translation: CAB14358.1 |
PIRi | B69961 |
RefSeqi | NP_390307.1, NC_000964.3 WP_003245985.1, NZ_JNCM01000036.1 |
Genome annotation databases
EnsemblBacteriai | CAB14358; CAB14358; BSU24270 |
GeneIDi | 938609 |
KEGGi | bsu:BSU24270 |
PATRICi | fig|224308.179.peg.2645 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D84432 Genomic DNA Translation: BAA12576.1 AL009126 Genomic DNA Translation: CAB14358.1 |
PIRi | B69961 |
RefSeqi | NP_390307.1, NC_000964.3 WP_003245985.1, NZ_JNCM01000036.1 |
3D structure databases
SMRi | P54523 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU24270 |
Proteomic databases
PaxDbi | P54523 |
PRIDEi | P54523 |
Genome annotation databases
EnsemblBacteriai | CAB14358; CAB14358; BSU24270 |
GeneIDi | 938609 |
KEGGi | bsu:BSU24270 |
PATRICi | fig|224308.179.peg.2645 |
Phylogenomic databases
eggNOGi | COG1154, Bacteria |
InParanoidi | P54523 |
OMAi | QVGYHAQ |
PhylomeDBi | P54523 |
Enzyme and pathway databases
UniPathwayi | UPA00064;UER00091 |
BioCyci | BSUB:BSU24270-MONOMER MetaCyc:BSU24270-MONOMER |
Family and domain databases
CDDi | cd02007, TPP_DXS, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
HAMAPi | MF_00315, DXP_synth, 1 hit |
InterProi | View protein in InterPro IPR005477, Dxylulose-5-P_synthase IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR005474, Transketolase_N |
PANTHERi | PTHR43322, PTHR43322, 1 hit |
Pfami | View protein in Pfam PF13292, DXP_synthase_N, 1 hit PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00204, dxs, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DXS_BACSU | |
Accessioni | P54523Primary (citable) accession number: P54523 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families