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C9TTT1 (C9TTT1_BRUPB) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315

EC=2.2.1.7 HAMAP-Rule MF_00315
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase HAMAP-Rule MF_00315
Gene names
Name:dxs HAMAP-Rule MF_00315 EMBL AEK53773.1
Ordered Locus Names:BPI_I466 EMBL AEK53773.1
ORF Names:BAHG_00761 EMBL EEX99831.1
OrganismBrucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94) [Complete proteome] [HAMAP] EMBL EEX99831.1
Taxonomic identifier520461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length643 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. SAAS SAAS005477 HAMAP-Rule MF_00315

Catalytic activity

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. SAAS SAAS005477 HAMAP-Rule MF_00315

Cofactor

Binds 1 magnesium ion per subunit By similarity. SAAS SAAS005477 HAMAP-Rule MF_00315

Binds 1 thiamine pyrophosphate per subunit By similarity. SAAS SAAS005477 HAMAP-Rule MF_00315

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. SAAS SAAS005477 HAMAP-Rule MF_00315

Subunit structure

Homodimer By similarity. SAAS SAAS005477 HAMAP-Rule MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily. HAMAP-Rule MF_00315

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region119 – 1213Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315
Region151 – 1522Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Sites

Metal binding1501Magnesium By similarity HAMAP-Rule MF_00315
Metal binding1791Magnesium By similarity HAMAP-Rule MF_00315
Binding site781Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site1791Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site2881Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site3701Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Sequences

Sequence LengthMass (Da)Tools
C9TTT1 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: 4948F8DD11A59F65

FASTA64369,153
        10         20         30         40         50         60 
MSRPSTPLLD KAPTPDRLRA LPEQDLPQLA EELRTELIDA VSTTGGHLGA GLGVVELTVA 

        70         80         90        100        110        120 
LHHVFNTPYD RIIWDVGHQA YPHKILTGRR DRIRTLRQAG GLSGFTKRAE SEYDPFGAAH 

       130        140        150        160        170        180 
SSTSISAGLG MAVASELSGE KRNVIAVIGD GSMSAGMAYE AMNNAGALDA RLIVILNDND 

       190        200        210        220        230        240 
MSIAPPTGAM SAYLARLVSG RTYRSVREAA KQVAQKLPKF LQDKARKSEE YARAFFTGGT 

       250        260        270        280        290        300 
LFEELGFYYV GPIDGHNLDH LLPVLKNVRD TQKGPVLIHV VTQKGKGYAP AEAAADKYHG 

       310        320        330        340        350        360 
VNEFDVITGK QAKPPANAPS YTKIFGTSLI EEARHDDKIV AVTAAMPTGT GLDLFGEAFP 

       370        380        390        400        410        420 
KRVFDVGIAE QHAVTFAAGL ASEGYKPFCA IYSTFLQRGY DQVVHDVSIQ NLPVRFPIDR 

       430        440        450        460        470        480 
AGLVGADGPT HAGSFDTGFL AALPGFVVMA ASDEAELRHM VRTAAEYDEG PISFRYPRGD 

       490        500        510        520        530        540 
GVGVDLPERG SVLEIGKGRI VREGTKVALL SFGTRLQECL AAAEELGAAG LSTTVADARF 

       550        560        570        580        590        600 
AKPLDHDLIR RLAREHEVLV MVEEGAVGGF GSHVLQFLAT DGLLDRGLKV RALTLPDIYQ 

       610        620        630        640 
DHGKPDAMYA EAGLDRTGIV RTVFAALHRD ELGHEALPTP FRA 

« Hide

References

« Hide 'large scale' references
[1]"The Genome Sequence of Brucella pinnipedialis B2/94."
The Broad Institute Genome Sequencing Platform
Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. expand/collapse author list , Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M., Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B2/94 EMBL EEX99831.1.
[2]Zygmunt M., Clockaert A.
Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B2/94 EMBL AEK53773.1.
[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: B2/94 EMBL AEK53773.1 and NCTC 12890 / BCCN 94-73 / B2/94.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002078 Genomic DNA. Translation: AEK53773.1.
DS999848 Genomic DNA. Translation: EEX99831.1.
RefSeqYP_004755541.1. NC_015857.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEK53773; AEK53773; BPI_I466.
EEX99831; EEX99831; BAHG_00761.
GeneID10996945.
KEGGbpp:BPI_I466.
PATRIC24250790. VBIBruPin17457_0401.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01662.

Enzyme and pathway databases

BioCycBPIN520461:GJF0-465-MONOMER.
UniPathwayUPA00064; UER00091.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPMF_00315. DXP_synth.
InterProIPR005477. 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]
PfamPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00204. dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC9TTT1_BRUPB
AccessionPrimary (citable) accession number: C9TTT1
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: June 11, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)