Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5I305 (A5I305_CLOBH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 43. 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·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

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

EC=2.2.1.7 HAMAP MF_00315
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase HAMAP MF_00315
Gene names
Name:dxs HAMAP MF_00315 EMBL CAL83422.1
Ordered Locus Names:CBO1881, CLC_1825
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length622 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 MF_00315

Catalytic activity

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

Cofactor

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

Subunit structure

Homodimer By similarity. SAAS SAAS005477 HAMAP MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily. HAMAP MF_00315

Sequences

Sequence LengthMass (Da)Tools
A5I305 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: D70DE95D8F4864EA

FASTA62268,669
        10         20         30         40         50         60 
MKMKNILDKY QDFDSIKSMS INELNQFSYE IREFLIDNVS KTGGHLASNL GVVELTLSIF 

        70         80         90        100        110        120 
NVFDLNKDKV IWDVGHQAYV HKILTGRKDK FNTLRQYGGL SGFPKICESP YDVFETGHSS 

       130        140        150        160        170        180 
TSISAALGMA RARDIKGENN KVIAVIGDGA LTGGMALEAL NDLGFNKTDL IIILNDNQMS 

       190        200        210        220        230        240 
IAENVGGMSS YLSKVRLDPT YNKLKKEVNN TLNKIPNVGK GMARSLERVK NGIKQMIVPG 

       250        260        270        280        290        300 
MLFENLGIKY LGPIDGHDIK ELSKVMKMAK NINGPVLIHT ITKKGKGYAY AEKKPDKFHG 

       310        320        330        340        350        360 
IGPFDCDSGE VNSKTCLTYS KVFGEELTKI AKEDKKVVAI TAAMKDGTGL RKFGETFPKR 

       370        380        390        400        410        420 
FFDVGIAEQH AVTLAAGIAT EGLKPVFAVY STFLQRAYDQ ILHDICIQNL PVVLGIDRAG 

       430        440        450        460        470        480 
IVGSDGETHQ GIFDLSYLSS LPNMTIIAPK CLEEMGIMLR WALNQNSPVA IRYPRGGDIK 

       490        500        510        520        530        540 
SLEMTPIKNM KKGKWEVICE EGDIAIIATG KMVQHAIIAR EKLKEYGIKS TIVNANFIKP 

       550        560        570        580        590        600 
IDKELIKNFV KKGYKIVTVE DNVIKGGFGS LVLQYISELK ANNTVLNLGF KDKFVPHGST 

       610        620 
DILYKIEGLD PEGIVKNIIK II 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger].
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A [Los Alamos].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38889.1.
AM412317 Genomic DNA. Translation: CAL83422.1.
RefSeqYP_001254383.1. NC_009495.1.
YP_001387680.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I305.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5I305.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5186136.
5401253.
GenomeReviewsGene locus CBO1881 in contig AM412317_GR.
Gene locus CLC_1825 in contig CP000727_GR.
KEGGcbh:CLC_1825.
cbo:CBO1881.
PATRIC19365821. VBICloBot22612_1853.

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHBG571647.
OMARAHEFES.
ProtClustDBPRK05444.

Family and domain databases

HAMAPMF_00315. DXP_synth.
[Tree]
InterProIPR005477. Dxylulose-5-P_synthase.
IPR011766. TPP_enzyme-bd_C.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK01662.
PfamPF02775. TPP_enzyme_C. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00204. Dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA5I305_CLOBH
AccessionPrimary (citable) accession number: A5I305
Secondary accession number(s): A7G4G5
Entry history
Integrated into UniProtKB/TrEMBL: June 26, 2007
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)