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Q5PMW8 (OTSA_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:SPA0940
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length473 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 – 473473Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
PRO_0000348917

Regions

Region21 – 222UDP-glucose binding By similarity
Region365 – 3695UDP-glucose binding By similarity

Sites

Binding site101Glucose-6-phosphate By similarity
Binding site761Glucose-6-phosphate By similarity
Binding site1301Glucose-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
Site851Involved in alpha anomer selectivity By similarity
Site1551Involved in alpha anomer selectivity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PMW8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E85B3F0AE58E144A

FASTA47353,581
        10         20         30         40         50         60 
MSRLVVVSNR IAPPDNKGGA GGLAVGVLGA LKAAGGLWFG WSGETGNEDE PLKKVTKGNI 

        70         80         90        100        110        120 
TWASFNLSEQ DYEDYYCQFS NAVLWPAFHY RLDLVQFQRP AWEGYMRVNA LLADKLLPLI 

       130        140        150        160        170        180 
KENDIIWVHD YHLLPFASEL RKRGVNNRIG FFLHIPFPTP EIFNALPPHD ELLEQLCDFD 

       190        200        210        220        230        240 
LLGFQTENDR LAFLDSLSSQ TRVTTRSGKQ HIAWGKDFQT EVYPIGIEPD EIALQAAGPL 

       250        260        270        280        290        300 
PPKLAQLKAE LKNVKNIFSV ERLDYSKGLP ERFLAYEALL ENYPQHRGKI RYTQIAPTSR 

       310        320        330        340        350        360 
GEVQAYQDIR HQLETEAGRI NGKYGQLGWT PLYYLNQHFD RKLLMKIFRY SDVGLVTPLR 

       370        380        390        400        410        420 
DGMNLVAKEF VAAQDPANPG VLVLSQFAGA ANELTSALIV NPYDRDDVAA ALNRALTMPL 

       430        440        450        460        470 
AERISRHAEM LDVIVKNDIN RWQERFIHDL KEVTPRSPER QQQNNVATFP KLA 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV76916.1.
RefSeqYP_150228.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PMW8.
SMRQ5PMW8. Positions 2-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA0940.

Proteomic databases

PRIDEQ5PMW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV76916; AAV76916; SPA0940.
PATRIC32351111. VBISalEnt134188_0992.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191478.
OMAIEFMPIH.
OrthoDBEOG6CCH1M.
ProtClustDBPRK10117.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-940-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_SALPA
AccessionPrimary (citable) accession number: Q5PMW8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 48 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