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Q2NTK9 (OTSA_SODGM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 49. 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:SG1241
OrganismSodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP]
Taxonomic identifier343509 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis

Protein attributes

Sequence length469 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 – 469469Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
PRO_0000348921

Regions

Region22 – 232UDP-glucose binding By similarity
Region365 – 3695UDP-glucose binding By similarity

Sites

Binding site101Glucose-6-phosphate By similarity
Binding site771Glucose-6-phosphate By similarity
Binding site1311Glucose-6-phosphate By similarity
Binding site2621UDP-glucose By similarity
Binding site2671UDP-glucose By similarity
Binding site3001Glucose-6-phosphate By similarity
Binding site3391UDP-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
Q2NTK9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 9E96324BCDDFDFF6

FASTA46953,446
        10         20         30         40         50         60 
MSRLVVVSNR IAAIEGKKES AGGLAVGIMD SLKDQGGLWF GWNGKISEED EPLEKNQQDN 

        70         80         90        100        110        120 
ITFAAFSLKQ SEYDQYYLNF SNTVIWPAFH YRLDLVQYQR EDYDGYCRVN EMLAGRLKPL 

       130        140        150        160        170        180 
VNEDDILWIH DYHLLPFAAA CRKLGMKNRI GFFLHIPFPT SEIFNALPPR KELLEKLCEY 

       190        200        210        220        230        240 
DLVGFQAESD RQAFIENLAL VTTVEDLDDD RIKAYNKLVT ARVYPIGVEP ESIRELAEGP 

       250        260        270        280        290        300 
LPPKLAHLRD KMNGQLIISV DRLDYSKGLP ERFQAYETLL ENYPQHRGNI RYFQIAPTSR 

       310        320        330        340        350        360 
GDVQAYQDIR HELETEAGRI NGHFSTLEWT PLFYLNQHYE RSLLMKIFRH CEVGLVTPLR 

       370        380        390        400        410        420 
DGMNLVAKEY VASQNPNDPG VLILSHFAGA ANELTSALLV NPYDRDGVAS ALDKALSMPL 

       430        440        450        460 
SERKARYQEM IAVIKQNDIV HWCQSFLDDL KKIPSKAEIV GQAVSGATR 

« Hide

References

[1]"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: morsitans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008232 Genomic DNA. Translation: BAE74516.1.
RefSeqYP_454921.1. NC_007712.1.

3D structure databases

ProteinModelPortalQ2NTK9.
SMRQ2NTK9. Positions 2-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING343509.SG1241.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE74516; BAE74516; SG1241.
GeneID3866764.
KEGGsgl:SG1241.
PATRIC23651168. VBISodGlo61428_2884.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
KOK00697.
OMAIEFMPIH.
OrthoDBEOG6CCH1M.
ProtClustDBPRK10117.

Enzyme and pathway databases

BioCycSGLO343509:GJJC-1291-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_SODGM
AccessionPrimary (citable) accession number: Q2NTK9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 7, 2006
Last modified: November 13, 2013
This is version 49 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