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A0PUT6 (OTSA_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trehalose-phosphate synthase

Short name=TPS
EC=2.4.1.-
Alternative name(s):
Trehalose-6-phosphate synthase
Gene names
Name:otsA
Ordered Locus Names:MUL_4052
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of glucose from a nucleoside diphosphate-glucose to glucose-6-phosphate to form trehalose-6-phosphate and nucleoside diphosphate By similarity.

Catalytic activity

Nucleoside diphosphate-glucose + D-glucose 6-phosphate = trehalose 6-phosphate + nucleoside diphosphate.

Pathway

Glycan biosynthesis; trehalose biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtrehalose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functiontransferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Trehalose-phosphate synthase
PRO_0000348924

Regions

Region48 – 492NDP-glucose binding By similarity
Region403 – 4075NDP-glucose binding By similarity

Sites

Binding site281Glucose-6-phosphate By similarity
Binding site1041Glucose-6-phosphate By similarity
Binding site1581Glucose-6-phosphate By similarity
Binding site3001NDP-glucose By similarity
Binding site3051NDP-glucose By similarity
Binding site3381Glucose-6-phosphate By similarity
Site1131Involved in alpha anomer selectivity By similarity
Site1831Involved in alpha anomer selectivity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PUT6 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 8F9B71DBA741915C

FASTA50056,100
        10         20         30         40         50         60 
MGPGGRQSAE PASTEVFGDS DFVVVANRLP VDQERLPDGT IAWKRSPGGL VTALEPLLRR 

        70         80         90        100        110        120 
RRGAWVGWAG VVENDVDVQD EPIVQDELQL QPVRLSADDV AQYYEGFSNA TLWPLYHDVI 

       130        140        150        160        170        180 
VRPIYHREWW DRYVDVNRRF AEATARAAAR GGTVWVQDYQ LQLVPKMLRA MRPDLTIGFF 

       190        200        210        220        230        240 
LHIPFPPVEL FMQLPWRTEI IQGLLGADLV GFHLPGGAQN FLILSRRLVG ADTSRGTVGV 

       250        260        270        280        290        300 
RSRFGEVILG SRTIRVGAFP ISIDSGALDQ TARDRNIRRR SREIRAELGN PRKILLGVDR 

       310        320        330        340        350        360 
LDYTKGIDVR LKAFSELLAE GRVKRDDTVL VQLATPSRER VESYQTLRND IERQVGHING 

       370        380        390        400        410        420 
EYAEVGHPVV HYLHRPVPRN ELIAFFVASD VMLVTPLRDG MNLVAKEYVA CRSDLGGALV 

       430        440        450        460        470        480 
LSEFTGAAAE LRHAYLVNPH DLEGVNDGIE EALNQTEEAG RRRMRSMRRQ VLAHDVDRWA 

       490        500 
RSFLDALADS RPNDSADAAD 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL06105.1.
RefSeqYP_907576.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PUT6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PUT6.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000074813; EBMYCP00000072818; EBMYCG00000074808.
GeneID4550106.
GenomeReviewsGene locus MUL_4052 in contig CP000325_GR.
KEGGmul:MUL_4052.
PATRIC18175808. VBIMycUlc37413_4715.

Organism-specific databases

GenoListMUL_4052.
CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
GeneTreeEBGT00050000016525.
HOGENOMHBG559076.
OMAEYGRKEM.
PhylomeDBA0PUT6.
ProtClustDBCLSK872185.

Family and domain databases

InterProIPR001830. Glyco_trans_20.
[Graphical view]
KOK00697.
PfamPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOTSA_MYCUA
AccessionPrimary (citable) accession number: A0PUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families