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Protein

Neutral trehalase

Gene

ntp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei283 – 2831SubstrateBy similarity
Binding sitei327 – 3271SubstrateBy similarity
Binding sitei336 – 3361SubstrateBy similarity
Binding sitei455 – 4551Substrate; via carbonyl oxygenBy similarity
Active sitei457 – 4571Proton donor/acceptorBy similarity
Active sitei652 – 6521Proton donor/acceptorBy similarity

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: PomBase
  • calcium ion binding Source: PomBase

GO - Biological processi

  • ascospore formation Source: PomBase
  • trehalose catabolic process Source: PomBase
  • trehalose catabolic process involved in cellular response to stress Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_322401. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral trehalase (EC:3.2.1.28)
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene namesi
Name:ntp1
ORF Names:SPBC660.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC660.07.
PomBaseiSPBC660.07. ntp1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Neutral trehalasePRO_0000173797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphothreonine1 Publication
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei50 – 501Phosphothreonine1 Publication
Modified residuei51 – 511Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO42893.

Interactioni

Protein-protein interaction databases

BioGridi277630. 32 interactions.
MINTiMINT-4673787.

Structurei

3D structure databases

ProteinModelPortaliO42893.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 2912Substrate bindingBy similarity
Regioni336 – 3383Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.Curated

Phylogenomic databases

HOGENOMiHOG000192885.
InParanoidiO42893.
KOiK01194.
OMAiWPPHQIM.
OrthoDBiEOG751NPZ.
PhylomeDBiO42893.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
IPR011120. Trehalase_Ca-bd.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
PF07492. Trehalase_Ca-bi. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSKFSSKYV DTEAISNDDD NPFATAKSYY SKDTDLSTRV SAGRPRTLST
60 70 80 90 100
SMEASAAPTI PELKNLRRRG SLDEHKQPRK FLVDVDKTLN ALLESEDTDR
110 120 130 140 150
NMQITIEDTG PKVVSLGSAS SGGYRLYELR GTYQLSNLLQ ELTLAKDYGR
160 170 180 190 200
RYILLDERRL NENPVNRLSR LIKGTFWDAL TRRIDASVLD VICRDTKDRS
210 220 230 240 250
GSHVNRIYVP KAEQEMYEYY VRAAKERPYL NLQVEYLPEE ITPEWVRDVN
260 270 280 290 300
DKPGLLALAM EKYQDDEGNT HLRGVPFVVP GGRFNELYGW DSYFESLGLL
310 320 330 340 350
VDDRVDLAKG MVENFIFEIT YYGKILNANR TYYLLRSQPP FLTDMALRVY
360 370 380 390 400
ERIKNEEGSL DFLHRAFSAT IKEYHTVWTA TPRLDPKTGL SRYRPGGLGI
410 420 430 440 450
PPETEASHFE HLLRPYMEKY HMTLEEFTHA YNYQQIHEPA LDEYFVHDRA
460 470 480 490 500
VRESGHDTTY RLEKVCADLA TVDLNSLLYK YETDISHVIL EYFDDKFVLP
510 520 530 540 550
NGTIETSAIW DRRARARRAA MEKYLWSEAD SMWYDYNTKL ETKSTYESAT
560 570 580 590 600
AFWALWAGVA TPRQAAKFVD VSLPKFEVAG GIVAGTKRSL GKVGLDNPSR
610 620 630 640 650
QWDYPNGWSP QQILAWYGLI RYGYEEETRR LVYRWLYTIT KSFVDFNGIV
660 670 680 690 700
VEKYDLTRPV DPHRVEAEYG NQGVNIKGVA REGFGWVNAS YEVGLTFCNS
710 720 730
HMRRALGACT TPDVFFAGIK EESLPAFENL SIHKN
Length:735
Mass (Da):84,603
Last modified:June 1, 1998 - v1
Checksum:i73FF979534E91BD4
GO

Sequence cautioni

The sequence BAA13934.1 differs from that shown. Reason: Frameshift at positions 556 and 643. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224339 Genomic DNA. Translation: CAA11904.1.
CU329671 Genomic DNA. Translation: CAA22527.1.
AB027837 Genomic DNA. Translation: BAA87141.1.
D89273 mRNA. Translation: BAA13934.1. Frameshift.
PIRiT40619.
T43203.
RefSeqiNP_595086.1. NM_001020993.2.

Genome annotation databases

EnsemblFungiiSPBC660.07.1; SPBC660.07.1:pep; SPBC660.07.
GeneIDi2541115.
KEGGispo:SPBC660.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224339 Genomic DNA. Translation: CAA11904.1.
CU329671 Genomic DNA. Translation: CAA22527.1.
AB027837 Genomic DNA. Translation: BAA87141.1.
D89273 mRNA. Translation: BAA13934.1. Frameshift.
PIRiT40619.
T43203.
RefSeqiNP_595086.1. NM_001020993.2.

3D structure databases

ProteinModelPortaliO42893.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277630. 32 interactions.
MINTiMINT-4673787.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Proteomic databases

MaxQBiO42893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC660.07.1; SPBC660.07.1:pep; SPBC660.07.
GeneIDi2541115.
KEGGispo:SPBC660.07.

Organism-specific databases

EuPathDBiFungiDB:SPBC660.07.
PomBaseiSPBC660.07. ntp1.

Phylogenomic databases

HOGENOMiHOG000192885.
InParanoidiO42893.
KOiK01194.
OMAiWPPHQIM.
OrthoDBiEOG751NPZ.
PhylomeDBiO42893.

Enzyme and pathway databases

ReactomeiREACT_322401. Digestion of dietary carbohydrate.

Miscellaneous databases

NextBioi20802228.
PROiO42893.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
IPR011120. Trehalase_Ca-bd.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
PF07492. Trehalase_Ca-bi. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the ntp1+ gene, encoding neutral trehalase in the fission yeast Schizosaccharomyces pombe."
    Soto T., Fernandez J., Dominguez A., Vicente-Soler J., Cansado J., Gacto M.
    Biochim. Biophys. Acta 1443:225-229(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 172-359, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  4. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-735.
    Strain: PR745.
  5. "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].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-49; THR-50 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTREA_SCHPO
AccessioniPrimary (citable) accession number: O42893
Secondary accession number(s): P78922, Q9UU37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: July 22, 2015
This is version 114 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.