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B1LQW0 (OTSA_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

EC=2.4.1.15
Alternative name(s):
Osmoregulatory trehalose synthesis protein A
Trehalose-6-phosphate synthase
UDP-glucose-glucosephosphate glucosyltransferase
Gene names
Name:otsA
Ordered Locus Names:EcSMS35_1289
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor By similarity.

Catalytic activity

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

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: UniProtKB-UniPathway

   Molecular_functionalpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
PRO_0000348895

Regions

Region22 – 232UDP-glucose binding By similarity
Region366 – 3705UDP-glucose binding By similarity

Sites

Binding site101Glucose-6-phosphate By similarity
Binding site771Glucose-6-phosphate By similarity
Binding site1311Glucose-6-phosphate By similarity
Binding site2631UDP-glucose By similarity
Binding site2681UDP-glucose By similarity
Binding site3011Glucose-6-phosphate By similarity
Binding site3401UDP-glucose; via amide nitrogen and carbonyl oxygen By similarity
Site861Involved in alpha anomer selectivity By similarity
Site1561Involved in alpha anomer selectivity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LQW0 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 63FFB6F938056F95

FASTA47453,611
        10         20         30         40         50         60 
MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN 

        70         80         90        100        110        120 
ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL 

       130        140        150        160        170        180 
LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY 

       190        200        210        220        230        240 
DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP 

       250        260        270        280        290        300 
LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS 

       310        320        330        340        350        360 
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL 

       370        380        390        400        410        420 
RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS 

       430        440        450        460        470 
LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000970 Genomic DNA. Translation: ACB19644.1.
RefSeqYP_001743347.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LQW0.
SMRB1LQW0. Positions 2-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_1289.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB19644; ACB19644; EcSMS35_1289.
GeneID6143857.
KEGGecm:EcSMS35_1289.
PATRIC18431443. VBIEscCol6161_1446.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191478.
KOK00697.
OMAWGESFVK.
OrthoDBEOG6CCH1M.

Enzyme and pathway databases

BioCycECOL439855:GHHB-1287-MONOMER.
UniPathwayUPA00299.

Family and domain databases

InterProIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsTIGR02400. trehalose_OtsA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameOTSA_ECOSM
AccessionPrimary (citable) accession number: B1LQW0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways