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Protein

Trehalose-phosphatase

Gene

tps2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process.

Catalytic activityi

Trehalose 6-phosphate + H2O = trehalose + phosphate.

Cofactori

Mg2+By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose-phosphatase (EC:3.1.3.12)
Alternative name(s):
Trehalose synthase complex catalytic subunit tps2
Trehalose-6-phosphate phosphatase
Short name:
TPP
Gene namesi
Name:tps2
ORF Names:SPAC3G6.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3G6.09c.
PomBaseiSPAC3G6.09c. tps2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 849849Trehalose-phosphatasePRO_0000316232Add
BLAST

Proteomic databases

MaxQBiO14145.

Interactioni

Protein-protein interaction databases

BioGridi279541. 23 interactions.
MINTiMINT-4670898.

Structurei

3D structure databases

ProteinModelPortaliO14145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 558558GlycosyltransferaseBy similarityAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 20 family.Curated
In the C-terminal section; belongs to the trehalose phosphatase family.Curated

Phylogenomic databases

HOGENOMiHOG000191477.
InParanoidiO14145.
KOiK16055.
OMAiETTSTHI.
OrthoDBiEOG76QFS6.
PhylomeDBiO14145.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.

Sequencei

Sequence statusi: Complete.

O14145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSGAQGNTQ SAAYKRIVNV SRNFQFKAAL NKDTREWTFQ HRSSGTALYS
60 70 80 90 100
AIASLGDPSS PWDAVYVASP GPVQISEGND HTVETKIDEA AVVHRSSSIV
110 120 130 140 150
ISPEDQEIFL KKATEYYRKK NIEADIVPVW GKVQRVPQAK SSSATITPSV
160 170 180 190 200
SNKLSTAYQS IKSEALKDGP MYADSVLWDV LHYRIPTLDG YQQHNLWKNF
210 220 230 240 250
TRWSQYFADN IVSNYRPGDL ILIHDYSLFL LPRLIRKQLS DAPIVFFLHA
260 270 280 290 300
PFCTSEVFRC LSKRAEILKG VLASNVIAMQ TDSYTRHFLS TCSNVLGLET
310 320 330 340 350
TSTHIDTSDG FRVVVFSSHV SIDVPRVYSR CNSKPVSLKI QQLKSLYPSD
360 370 380 390 400
KKLIVGRDQL TKACGVTHKL RAFRELLIHF PKWRGHVVLI QITSLPVGNN
410 420 430 440 450
YSNEELKKTE NLVAQINSEF GSLDYTPVIH FHQLLDPDEY YALLSVANIA
460 470 480 490 500
CVSSVRDSMN TMALEYVACQ QKNKGSLILS EFSGTAELLL SAYLVNPYDY
510 520 530 540 550
SRFAETINYC LNMTEKERER RFSSLWKQAT SQSSQQWIYK LINRAAYEVK
560 570 580 590 600
ALESHMTTPL LTYNILIKPY RNAKRRLFLL DYDGTLIESA RNSIDAVPTD
610 620 630 640 650
RLLRTLKRLA SDSRNIVWIL SGRSQKFMEE WMGDISELGL SSEHGSAIRP
660 670 680 690 700
PLAGSWSSCA ENLDLSWKDT VRDFFQYYVE RTPGSYIEEK KHSISWCYQN
710 720 730 740 750
ANTTYSKFQS LECQTNLEDM LKHYDVEISP AKSFLEVHPN YLNKGSIVRR
760 770 780 790 800
ILKRSGSVDF VFCAGDDKTD ENMFEVFLPT AFSNSHLIDE IDSTEYSGSH
810 820 830 840
HTDDNSDANK VENVKVATFR VHIGLTDKPT LSDYHLPAPR DLGELLHNL
Length:849
Mass (Da):96,341
Last modified:January 1, 1998 - v1
Checksum:i6C7F74E43A6EBDFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16285.1.
PIRiT38728.
RefSeqiNP_594975.1. NM_001020406.2.

Genome annotation databases

EnsemblFungiiSPAC3G6.09c.1; SPAC3G6.09c.1:pep; SPAC3G6.09c.
GeneIDi2543109.
KEGGispo:SPAC3G6.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16285.1.
PIRiT38728.
RefSeqiNP_594975.1. NM_001020406.2.

3D structure databases

ProteinModelPortaliO14145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279541. 23 interactions.
MINTiMINT-4670898.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Proteomic databases

MaxQBiO14145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3G6.09c.1; SPAC3G6.09c.1:pep; SPAC3G6.09c.
GeneIDi2543109.
KEGGispo:SPAC3G6.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC3G6.09c.
PomBaseiSPAC3G6.09c. tps2.

Phylogenomic databases

HOGENOMiHOG000191477.
InParanoidiO14145.
KOiK16055.
OMAiETTSTHI.
OrthoDBiEOG76QFS6.
PhylomeDBiO14145.

Miscellaneous databases

PROiO14145.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPS2_SCHPO
AccessioniPrimary (citable) accession number: O14145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 95 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.