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

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Q50000 (DXS_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. 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
Synonyms:	tktB
Ordered Locus Names:	ML1038

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	643 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 MF_00315
Catalytic activity	Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO₂. HAMAP MF_00315
Cofactor	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 MF_00315
Subunit structure	Homodimer By similarity. HAMAP MF_00315
Sequence similarities	Belongs to the transketolase family. DXPS subfamily.
Sequence caution	The sequence AAA62954.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Isoprene biosynthesis Thiamine biosynthesis
Ligand	Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	terpenoid biosynthetic process Inferred from electronic annotation. Source: InterPro thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-deoxy-D-xylulose-5-phosphate synthase activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 643

643

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

PRO_0000189129

Sequences

Sequence

Length

Mass (Da)

Tools

Q50000 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 2C86C884ABCAA00B
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FASTA

643

68,863

        10         20         30         40         50         60 
MLEQIRRPAD LQHLSQQQLR DLAAEIRELL VHKVAATGGH LGPNLGVVEL TLALHRVFDS 

        70         80         90        100        110        120 
PHDPIIFDTG HQAYVHKMLT GRCQDFDSLR KKAGLSGYPS RAESEHDWVE SSHASTALSY 

       130        140        150        160        170        180 
ADGLAKAFEL AGNRNRHVVA VVGDGALTGG MCWEALNNIA ATPRPVVIVV NDNGRSYAPT 

       190        200        210        220        230        240 
IGGVADHLAT LRLQPAYERL LEKGRDALHS LPLIGQIAYR FMHSVKAGIK DSLSPQLLFT 

       250        260        270        280        290        300 
DLGLKYVGPV DGHDEHAVEV ALRKARGFGG PVIVHVVTRK GMGYPPAEAD QAEQMHTCGV 

       310        320        330        340        350        360 
MDPTTGQPTK IAAPDWTAIF SDALIGYAMK RRDIVAITAA MPGPTGLTAF GQCFPDRLFD 

       370        380        390        400        410        420 
VGIAEQHAMT SAAGLAMGRM HPVVAIYSTF LNRAFDQIMM DVALHKLPVT MVIDRAGITG 

       430        440        450        460        470        480 
SDGPSHNGMW DLSMLGIVPG MRVAAPRDAI RLREELGEAL DVDDGPTAIR FPKGDVCEDI 

       490        500        510        520        530        540 
PALKRRSGVD VLAVPATGLA QDVLLVGVGV FASMALAVAK RLHNQGIGVT VIDPRWVLPV 

       550        560        570        580        590        600 
CDGVLELAHT HKLIVTLEDN GVNGGVGAAV STALRQVEID TPCRDVGLPQ EFYDHASRSE 

       610        620        630        640 
VLADLGLTDQ DVARRITGWV VAFGHCGSGD DAGQYGPRSS QTM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15181 Genomic DNA. Translation: AAA62954.1. Different initiation. AL583920 Genomic DNA. Translation: CAC31419.1.
PIR	H87038.
RefSeq	NP_301766.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q50000.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000029318; EBMYCP00000028924; EBMYCG00000029313.
GeneID	910120.
GenomeReviews	Gene locus ML1038 in contig AL450380_GR.
KEGG	mle:ML1038.
NMPDR	fig\|272631.1.peg.638.
PATRIC	18053848. VBIMycLep78757_1869.
Organism-specific databases
Leproma	ML1038.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016269.
HOGENOM	HBG571647.
OMA	QYDISYM.
ProtClustDB	PRK05444.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1038-MONOMER.
Family and domain databases
HAMAP	MF_00315. DXP_synth. [Tree]
InterPro	IPR005477. 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]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KO	K01662.
Pfam	PF02775. TPP_enzyme_C. 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...

Entry information

Entry name

DXS_MYCLE

Accession

Primary (citable) accession number: Q50000

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	January 25, 2012
This is version 85 of the entry and version 2 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents