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P40387

- TPS1_SCHPO

UniProt

P40387 - TPS1_SCHPO

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Protein

Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

Gene
tps1, SPAC328.03
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Appears to have a role in spore germination. In S.pombe it appears to have no role in the control of the initial steps of glycolysis.

Catalytic activityi

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

GO - Molecular functioni

  1. alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Source: PomBase
  2. protein binding Source: PomBase

GO - Biological processi

  1. ascospore formation Source: PomBase
  2. cellular response to desiccation Source: PomBase
  3. cellular response to ethanol Source: PomBase
  4. cellular response to freezing Source: PomBase
  5. cellular response to heat Source: PomBase
  6. positive regulation of trehalose catabolic process Source: PomBase
  7. trehalose biosynthesis in response to heat stress Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Stress response

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC:2.4.1.15)
Alternative name(s):
Trehalose-6-phosphate synthase
UDP-glucose-glucosephosphate glucosyltransferase
Gene namesi
Name:tps1
ORF Names:SPAC328.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC328.03.

Subcellular locationi

GO - Cellular componenti

  1. alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Source: PomBase
  2. cytosol Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Alpha,alpha-trehalose-phosphate synthase [UDP-forming]PRO_0000122500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401Phosphotyrosine1 Publication
Modified residuei503 – 5031Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40387.
PaxDbiP40387.

Expressioni

Inductioni

By heat shock.

Interactioni

Protein-protein interaction databases

BioGridi279113. 93 interactions.
MINTiMINT-4689743.
STRINGi4896.SPAC328.03-1.

Structurei

3D structure databases

ProteinModelPortaliP40387.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0380.
HOGENOMiHOG000191477.
KOiK00697.
OMAiWGESFVK.
OrthoDBiEOG76QFS6.
PhylomeDBiP40387.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.

Sequencei

Sequence statusi: Complete.

P40387-1 [UniParc]FASTAAdd to Basket

« Hide

MSDAHDTIKS LTGDASNSRR LIVVSNRLPI TIKRKDNGTY DFSMSSGGLV    50
SALSGLKKLM TFQWLGWCGQ EIPEDEKPMI IQRLQDECSA IPVFLDDETA 100
DRHYNGFSNS ILWPLFHYHP GEINFDEENW EAYRAANYAF AEAIVKNLQD 150
GDLIWVQDYH LMVLPQMLRE LIGDKFKDIK IGFFLHTPFP SSEIYRVLPV 200
RNEILEGVLN CDLVGFHTYD YARHFLSACS RILNLSTLPN GVEYNGQMVS 250
VGTFPIGIDP EKFSDALKSD VVKDRIASIE RRLQGVKVIV GVDRLDYIKG 300
VPQKFHAFEV FLEQYPEWVG KVVLVQVAVP SRQDVEEYQN LRAVVNELVG 350
RINGRFGTVE YTPIHFLHKS VRFEELVALY NVSDVCLITS TRDGMNLVSY 400
EYICTQQERH GALILSEFAG AAQSLNGSIV INPWNTEELA NSIHDALTMP 450
EKQREANENK LFRYVNKYTS QFWGQSFVGE LQRIQHYSHP HPRRTNPILR 500
TKSAQVLSMN SSS 513
Length:513
Mass (Da):58,493
Last modified:August 14, 2001 - v2
Checksum:i9FC247B626CE2B00
GO

Sequence cautioni

The sequence CAA82861.1 differs from that shown. Reason: Frameshift at position 475.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771A → R in CAA82861. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29971 Genomic DNA. Translation: CAA82861.1. Frameshift.
CU329670 Genomic DNA. Translation: CAB95998.1.
PIRiT46564.
RefSeqiNP_594205.1. NM_001019628.2.

Genome annotation databases

EnsemblFungiiSPAC328.03.1; SPAC328.03.1:pep; SPAC328.03.
GeneIDi2542660.
KEGGispo:SPAC328.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29971 Genomic DNA. Translation: CAA82861.1 . Frameshift.
CU329670 Genomic DNA. Translation: CAB95998.1 .
PIRi T46564.
RefSeqi NP_594205.1. NM_001019628.2.

3D structure databases

ProteinModelPortali P40387.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 279113. 93 interactions.
MINTi MINT-4689743.
STRINGi 4896.SPAC328.03-1.

Protein family/group databases

CAZyi GT20. Glycosyltransferase Family 20.

Proteomic databases

MaxQBi P40387.
PaxDbi P40387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC328.03.1 ; SPAC328.03.1:pep ; SPAC328.03 .
GeneIDi 2542660.
KEGGi spo:SPAC328.03.

Organism-specific databases

PomBasei SPAC328.03.

Phylogenomic databases

eggNOGi COG0380.
HOGENOMi HOG000191477.
KOi K00697.
OMAi WGESFVK.
OrthoDBi EOG76QFS6.
PhylomeDBi P40387.

Miscellaneous databases

NextBioi 20803708.
PROi P40387.

Family and domain databases

InterProi IPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view ]
Pfami PF00982. Glyco_transf_20. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02400. trehalose_OtsA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe."
    Blazquez M.A., Stucka R., Feldmann H., Gancedo C.
    J. Bacteriol. 176:3895-3902(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 AND SER-503, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTPS1_SCHPO
AccessioniPrimary (citable) accession number: P40387
Secondary accession number(s): Q9P3U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: August 14, 2001
Last modified: June 11, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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