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C9TTT1

- C9TTT1_BRUPB

UniProt

C9TTT1 - C9TTT1_BRUPB

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Protein

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

Gene

dxs

Organism
Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94)
Status
Unreviewed - 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 annotationSAAS annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Note: Binds 1 magnesium ion per subunit.UniRule annotationSAAS annotation
  • Note: Binds 1 thiamine pyrophosphate per subunit.UniRule annotationSAAS 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

TransferaseUniRule annotationSAAS annotation

Keywords - Biological processi

Isoprene biosynthesisUniRule annotationSAAS annotation, Thiamine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Thiamine pyrophosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciBPIN520461:GJF0-465-MONOMER.
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
Gene namesi
Name:dxsUniRule annotationImported
Ordered Locus Names:BPI_I466Imported
ORF Names:BAHG_00761Imported
OrganismiBrucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94)Imported
Taxonomic identifieri520461 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000010095: Chromosome 1

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

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

KOiK01662.

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.

C9TTT1-1 [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
VNEFDVITGK QAKPPANAPS 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):69,153
Last modified:November 24, 2009 - v1
Checksum:i4948F8DD11A59F65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002078 Genomic DNA. Translation: AEK53773.1.
DS999848 Genomic DNA. Translation: EEX99831.1.
RefSeqiYP_004755541.1. NC_015857.1.

Genome annotation databases

EnsemblBacteriaiAEK53773; AEK53773; BPI_I466.
EEX99831; EEX99831; BAHG_00761.
GeneIDi10996945.
KEGGibpp:BPI_I466.
PATRICi24250790. VBIBruPin17457_0401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002078 Genomic DNA. Translation: AEK53773.1 .
DS999848 Genomic DNA. Translation: EEX99831.1 .
RefSeqi YP_004755541.1. NC_015857.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEK53773 ; AEK53773 ; BPI_I466 .
EEX99831 ; EEX99831 ; BAHG_00761 .
GeneIDi 10996945.
KEGGi bpp:BPI_I466.
PATRICi 24250790. VBIBruPin17457_0401.

Phylogenomic databases

KOi K01662.

Enzyme and pathway databases

UniPathwayi UPA00064 ; UER00091 .
BioCyci BPIN520461:GJF0-465-MONOMER.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPi MF_00315. DXP_synth.
InterProi IPR005477. 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 ]
Pfami PF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00204. dxs. 1 hit.
PROSITEi PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B2/94Imported.
  2. Zygmunt M., Clockaert A.
    Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B2/94Imported.
  3. "The genome sequence of Brucella pinnipedialis B2/94 sheds light on the evolutionary history of the genus Brucella."
    Audic S., Lescot M., Claverie J.M., Cloeckaert A., Zygmunt M.S.
    BMC Evol. Biol. 11:200-200(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B2/94Imported and NCTC 12890 / BCCN 94-73 / B2/94Imported.

Entry informationi

Entry nameiC9TTT1_BRUPB
AccessioniPrimary (citable) accession number: C9TTT1
Entry historyi
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: November 26, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3