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Protein

Trehalose-6-phosphate synthase

Gene

otsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength.4 Publications

Catalytic activityi

UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.2 Publications

Enzyme regulationi

Activated by potassium and other monovalent cations at 0.25 M, but partially inhibited at greater concentrations (PubMed:3131312). Inhibited by validoxylamine A 6'-O-phosphate (PubMed:20077550).2 Publications

Kineticsi

Kcat is 34 sec(-1) for glucosyltransferase activity.1 Publication
  1. KM=1.7 mM for UDP-Glc1 Publication
  2. KM=7.3 mM for Glc-6-P1 Publication

    Pathwayi: trehalose biosynthesis

    This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei10D-glucose 6-phosphateCombined sources2 Publications1
    Binding sitei77D-glucose 6-phosphateCombined sources2 Publications1
    Sitei86Involved in alpha anomer selectivity1 Publication1
    Binding sitei131D-glucose 6-phosphateCombined sources2 Publications1
    Sitei156Involved in alpha anomer selectivity1 Publication1
    Binding sitei263UDP-glucoseCombined sources3 Publications1
    Binding sitei268UDP-glucoseCombined sources3 Publications1
    Binding sitei301D-glucose 6-phosphateCombined sources2 Publications1
    Binding sitei340UDP-glucose; via amide nitrogen and carbonyl oxygenCombined sources3 Publications1

    GO - Molecular functioni

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • response to osmotic stress Source: EcoCyc
    • trehalose biosynthetic process Source: EcoCyc
    • trehalose metabolism in response to cold stress Source: EcoCyc

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    Biological processStress response
    LigandPotassium

    Enzyme and pathway databases

    BioCyciEcoCyc:TREHALOSE6PSYN-MONOMER
    MetaCyc:TREHALOSE6PSYN-MONOMER
    UniPathwayiUPA00299

    Protein family/group databases

    CAZyiGT20 Glycosyltransferase Family 20

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose-6-phosphate synthase1 Publication (EC:2.4.1.152 Publications)
    Short name:
    TPS1 Publication
    Alternative name(s):
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming]Curated
    Osmoregulatory trehalose synthesis protein A1 Publication
    Short name:
    OtsA1 Publication
    UDP-glucose-glucosephosphate glucosyltransferaseCurated
    Gene namesi
    Name:otsA1 Publication
    Ordered Locus Names:b1896, JW5312
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11751 otsA

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Disruption phenotypei

    Mutants are viable, but osmotically sensitive in minimal media and sensitive to cold shock.1 Publication

    Chemistry databases

    DrugBankiDB02007 alpha-D-glucose 6-phosphate
    DB01861 Uridine diphosphate glucose
    DB03435 Uridine-5'-Diphosphate
    DB03488 Uridine-5'-Diphosphate-2-Deoxy-2-Fluoro-Alpha-D-Galactose

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001224892 – 474Trehalose-6-phosphate synthaseAdd BLAST473

    Proteomic databases

    PaxDbiP31677
    PRIDEiP31677

    Expressioni

    Inductioni

    By cold-shock, osmotic-shock and during the transition to stationary phase. Expression is partially dependent on RpoS.4 Publications

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi4259473, 16 interactors
    DIPiDIP-10417N
    IntActiP31677, 10 interactors
    STRINGi316385.ECDH10B_2037

    Structurei

    Secondary structure

    1474
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 10Combined sources7
    Helixi16 – 18Combined sources3
    Helixi23 – 35Combined sources13
    Beta strandi37 – 47Combined sources11
    Beta strandi54 – 58Combined sources5
    Beta strandi61 – 68Combined sources8
    Helixi70 – 76Combined sources7
    Turni77 – 79Combined sources3
    Helixi80 – 83Combined sources4
    Helixi85 – 89Combined sources5
    Helixi93 – 95Combined sources3
    Helixi100 – 117Combined sources18
    Helixi118 – 120Combined sources3
    Beta strandi126 – 131Combined sources6
    Helixi132 – 134Combined sources3
    Helixi137 – 143Combined sources7
    Beta strandi150 – 153Combined sources4
    Helixi161 – 164Combined sources4
    Helixi170 – 177Combined sources8
    Beta strandi180 – 187Combined sources8
    Helixi188 – 201Combined sources14
    Beta strandi204 – 207Combined sources4
    Turni208 – 210Combined sources3
    Beta strandi211 – 214Combined sources4
    Beta strandi217 – 223Combined sources7
    Helixi230 – 238Combined sources9
    Helixi243 – 251Combined sources9
    Turni252 – 254Combined sources3
    Beta strandi256 – 261Combined sources6
    Helixi266 – 268Combined sources3
    Helixi270 – 283Combined sources14
    Helixi285 – 287Combined sources3
    Turni288 – 290Combined sources3
    Beta strandi291 – 296Combined sources6
    Helixi305 – 325Combined sources21
    Beta strandi332 – 336Combined sources5
    Helixi342 – 351Combined sources10
    Beta strandi353 – 357Combined sources5
    Beta strandi360 – 363Combined sources4
    Helixi366 – 374Combined sources9
    Beta strandi382 – 386Combined sources5
    Helixi390 – 393Combined sources4
    Beta strandi398 – 401Combined sources4
    Helixi406 – 417Combined sources12
    Helixi421 – 437Combined sources17
    Helixi440 – 453Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1GZ5X-ray2.43A/B/C/D2-457[»]
    1UQTX-ray2.00A/B2-474[»]
    1UQUX-ray2.00A/B2-474[»]
    2WTXX-ray2.20A/B/C/D1-474[»]
    ProteinModelPortaliP31677
    SMRiP31677
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31677

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni22 – 23UDP-glucose bindingCombined sources3 Publications2
    Regioni366 – 370UDP-glucose bindingCombined sources3 Publications5

    Sequence similaritiesi

    Belongs to the glycosyltransferase 20 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C1K Bacteria
    COG0380 LUCA
    HOGENOMiHOG000191478
    InParanoidiP31677
    KOiK00697
    OMAiIEFMPIH
    PhylomeDBiP31677

    Family and domain databases

    CDDicd03788 GT1_TPS, 1 hit
    InterProiView protein in InterPro
    IPR001830 Glyco_trans_20
    IPR012766 Trehalose_OtsA
    PfamiView protein in Pfam
    PF00982 Glyco_transf_20, 1 hit
    TIGRFAMsiTIGR02400 trehalose_OtsA, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31677-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED
    60 70 80 90 100
    QPLKKVKKGN ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR
    110 120 130 140 150
    PAWDGYLRVN ALLADKLLPL LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI
    160 170 180 190 200
    GFFLHIPFPT PEIFNALPTY DTLLEQLCDY DLLGFQTEND RLAFLDCLSN
    210 220 230 240 250
    LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP LPPKLAQLKA
    260 270 280 290 300
    ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS
    310 320 330 340 350
    RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR
    360 370 380 390 400
    YSDVGLVTPL RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI
    410 420 430 440 450
    VNPYDRDEVA AALDRALTMS LAERISRHAE MLDVIVKNDI NHWQECFISD
    460 470
    LKQIVPRSAE SQQRDKVATF PKLA
    Length:474
    Mass (Da):53,611
    Last modified:January 23, 2007 - v3
    Checksum:i63FFB6F938056F95
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X69160 Genomic DNA Translation: CAA48913.1
    U00096 Genomic DNA Translation: AAC74966.1
    AP009048 Genomic DNA Translation: BAA15717.2
    U27211 Genomic DNA Translation: AAA68604.1
    PIRiI83402
    RefSeqiNP_416410.1, NC_000913.3
    WP_001295646.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74966; AAC74966; b1896
    BAA15717; BAA15717; BAA15717
    GeneIDi946405
    KEGGiecj:JW5312
    eco:b1896
    PATRICifig|1411691.4.peg.353

    Similar proteinsi

    Entry informationi

    Entry nameiOTSA_ECOLI
    AccessioniPrimary (citable) accession number: P31677
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 140 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health