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Protein

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

Gene

dxs

Organism
Brucella suis biovar 1 (strain 1330)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781Thiamine pyrophosphateUniRule annotation
Metal bindingi150 – 1501MagnesiumUniRule annotation
Metal bindingi179 – 1791MagnesiumUniRule annotation
Binding sitei179 – 1791Thiamine pyrophosphateUniRule annotation
Binding sitei288 – 2881Thiamine pyrophosphateUniRule annotation
Binding sitei370 – 3701Thiamine pyrophosphateUniRule annotation

GO - Molecular functioni

  1. 1-deoxy-D-xylulose-5-phosphate synthase activity Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. thiamine pyrophosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 1-deoxy-D-xylulose 5-phosphate biosynthetic process Source: UniProtKB-UniPathway
  2. terpenoid biosynthetic process Source: UniProtKB-HAMAP
  3. thiamine biosynthetic process Source: UniProtKB-HAMAP
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:BS1330_I0437, BR0436
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000824: Chromosome I, UP000007104: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6436431-deoxy-D-xylulose-5-phosphate synthasePRO_0000189093Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204722.BR0436.

Structurei

3D structure databases

ProteinModelPortaliQ8G292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 1213Thiamine pyrophosphate bindingUniRule annotation
Regioni151 – 1522Thiamine pyrophosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1154.
HOGENOMiHOG000012988.
KOiK01662.
OMAiCIPNMVV.
OrthoDBiEOG6BKJ6P.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth.
InterProiIPR005477. 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]
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.

Q8G292-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRPSTPLLD KAPTPDRLRA LPEQDLPQLA EELRTELIDA VSTTGGHLGA
60 70 80 90 100
GLGVVELTVA LHHVFNTPYD RIIWDVGHQA YPHKILTGRR DRIRTLRQAG
110 120 130 140 150
GLSGFTKRAE SEYDPFGAAH SSTSISAGLG MAVASELSGE KRNVIAVIGD
160 170 180 190 200
GSMSAGMAYE AMNNAGALDA RLIVILNDND MSIAPPTGAM SAYLARLVSG
210 220 230 240 250
RTYRSVREAA KQVAQKLPKF LQDKARKSEE YARAFFTGGT LFEELGFYYV
260 270 280 290 300
GPIDGHNLDH LLPVLKNVRD TQKGPVLIHV VTQKGKGYAP AEAAADKYHG
310 320 330 340 350
VNKFDVITGK QAKPPANVPS YTKIFGTSLI EEARHDDKIV AVTAAMPTGT
360 370 380 390 400
GLDLFGEAFP KRVFDVGIAE QHAVTFAAGL ASEGYKPFCA IYSTFLQRGY
410 420 430 440 450
DQVVHDVSIQ NLPVRFPIDR AGLVGADGPT HAGSFDTGFL AALPGFVVMA
460 470 480 490 500
ASDEAELRHM VRTAAEYDEG PISFRYPRGD GVGVDLPERG SVLEIGKGRI
510 520 530 540 550
VREGTKVALL SFGTRLQECL AAAEELGAAG LSTTVADARF AKPLDHDLIR
560 570 580 590 600
RLAREHEVLV MVEEGAVGGF GSHVLQFLAT DGLLDRGLKV RALTLPDIYQ
610 620 630 640
DHGKPDAMYA EAGLDRTGIV RTVFAALHRD ELGHEALPTP FRA
Length:643
Mass (Da):69,180
Last modified:March 1, 2003 - v1
Checksum:iE42DFB422D129FEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29379.1.
CP002997 Genomic DNA. Translation: AEM17792.1.
RefSeqiNP_697464.1. NC_004310.3.
YP_005615284.1. NC_017251.1.

Genome annotation databases

EnsemblBacteriaiAAN29379; AAN29379; BR0436.
AEM17792; AEM17792; BS1330_I0437.
GeneIDi1166097.
12136756.
KEGGibms:BR0436.
bsi:BS1330_I0437.
PATRICi17789166. VBIBruSui107850_0451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29379.1.
CP002997 Genomic DNA. Translation: AEM17792.1.
RefSeqiNP_697464.1. NC_004310.3.
YP_005615284.1. NC_017251.1.

3D structure databases

ProteinModelPortaliQ8G292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi204722.BR0436.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN29379; AAN29379; BR0436.
AEM17792; AEM17792; BS1330_I0437.
GeneIDi1166097.
12136756.
KEGGibms:BR0436.
bsi:BS1330_I0437.
PATRICi17789166. VBIBruSui107850_0451.

Phylogenomic databases

eggNOGiCOG1154.
HOGENOMiHOG000012988.
KOiK01662.
OMAiCIPNMVV.
OrthoDBiEOG6BKJ6P.

Enzyme and pathway databases

UniPathwayiUPA00064; UER00091.

Miscellaneous databases

PROiQ8G292.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth.
InterProiIPR005477. 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]
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiDXS_BRUSU
AccessioniPrimary (citable) accession number: Q8G292
Secondary accession number(s): G0K6Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: January 7, 2015
This is version 79 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. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.