1-deoxy-D-xylulose-5-phosphate synthase - Mycobacterium bovis (strain BCG / Pasteur 1173P2)

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A1KM20 (DXS_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1-deoxy-D-xylulose-5-phosphate synthase
EC=2.2.1.7

Alternative name(s):
1-deoxyxylulose-5-phosphate synthase
Short name=DXP synthase
Short name=DXPS

Gene names

Name:	dxs
Ordered Locus Names:	BCG_2695c

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Inferred 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. HAMAP-Rule MF_00315
Catalytic activity	Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO₂. HAMAP-Rule MF_00315
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
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. HAMAP-Rule MF_00315
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the transketolase family. DXPS subfamily.

Ontologies

Keywords
Biological process	Isoprene biosynthesis Thiamine biosynthesis
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamine pyrophosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 638

638

1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315

PRO_1000019040

Regions

Region

112 – 114

Thiamine pyrophosphate binding By similarity

Region

145 – 146

Thiamine pyrophosphate binding By similarity

Sites

Metal binding

144

Magnesium By similarity

Metal binding

173

Magnesium By similarity

Binding site

Thiamine pyrophosphate By similarity

Binding site

173

Thiamine pyrophosphate By similarity

Binding site

284

Thiamine pyrophosphate By similarity

Binding site

365

Thiamine pyrophosphate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A1KM20 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6F8DC2A78290873F
Show »

FASTA

638

67,885

        10         20         30         40         50         60 
MLQQIRGPAD LQHLSQAQLR ELAAEIREFL IHKVAATGGH LGPNLGVVEL TLALHRVFDS 

        70         80         90        100        110        120 
PHDPIIFDTG HQAYVHKMLT GRSQDFATLR KKGGLSGYPS RAESEHDWVE SSHASAALSY 

       130        140        150        160        170        180 
ADGLAKAFEL TGHRNRHVVA VVGDGALTGG MCWEALNNIA ASRRPVIIVV NDNGRSYAPT 

       190        200        210        220        230        240 
IGGVADHLAT LRLQPAYEQA LETGRDLVRA VPLVGGLWFR FLHSVKAGIK DSLSPQLLFT 

       250        260        270        280        290        300 
DLGLKYVGPV DGHDERAVEV ALRSARRFGA PVIVHVVTRK GMGYPPAEAD QAEQMHSTVP 

       310        320        330        340        350        360 
IDPATGQATK VAGPGWTATF SDALIGYAQK RRDIVAITAA MPGPTGLTAF GQRFPDRLFD 

       370        380        390        400        410        420 
VGIAEQHAMT SAAGLAMGGL HPVVAIYSTF LNRAFDQIMM DVALHKLPVT MVLDRAGITG 

       430        440        450        460        470        480 
SDGASHNGMW DLSMLGIVPG IRVAAPRDAT RLREELGEAL DVDDGPTALR FPKGDVGEDI 

       490        500        510        520        530        540 
SALERRGGVD VLAAPADGLN HDVLLVAIGA FAPMALAVAK RLHNQGIGVT VIDPRWVLPV 

       550        560        570        580        590        600 
SDGVRELAVQ HKLLVTLEDN GVNGGAGSAV SAALRRAEID VPCRDVGLPQ EFYEHASRSE 

       610        620        630 
VLADLGLTDQ DVARRITGWV AALGTGVCAS DAIPEHLD

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References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy."
Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.
Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL72683.1.
RefSeq	YP_978781.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KM20.
SMR	A1KM20. Positions 1-607.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_2695c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL72683; CAL72683; BCG_2695c.
GeneID	4699174.
KEGG	mbb:BCG_2695c.
PATRIC	18016380. VBIMycBov80988_2936.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1154.
HOGENOM	HOG000012986.
KO	K01662.
OMA	PVAYHGP.
ProtClustDB	PRK05444.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-2735-MONOMER.
UniPathway	UPA00064; UER00091.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
HAMAP	MF_00315. DXP_synth.
InterPro	IPR005477. Dxylulose-5-P_synthase. 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]
Pfam	PF13292. DXP_synthase_N. 1 hit. PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
TIGRFAMs	TIGR00204. dxs. 1 hit.
PROSITE	PS00801. TRANSKETOLASE_1. 1 hit. PS00802. TRANSKETOLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	A1KM20.

Entry information

Entry name

DXS_MYCBP

Accession

Primary (citable) accession number: A1KM20

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents