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Protein

Probable trehalase

Gene

NTH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei331 – 3311SubstrateBy similarity
Binding sitei375 – 3751SubstrateBy similarity
Binding sitei384 – 3841SubstrateBy similarity
Binding sitei505 – 5051Substrate; via carbonyl oxygenBy similarity
Active sitei507 – 5071Proton donor/acceptorBy similarity
Active sitei703 – 7031Proton donor/acceptorBy similarity

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: SGD
  • calcium ion binding Source: InterPro

GO - Biological processi

  • trehalose catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17147.
YEAST:YBR001C-MONOMER.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable trehalase (EC:3.2.1.28)
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene namesi
Name:NTH2
Ordered Locus Names:YBR001C
ORF Names:YBR0106
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR001C.
SGDiS000000205. NTH2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780Probable trehalasePRO_0000173800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei88 – 881PhosphothreonineCombined sources
Modified residuei112 – 1121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35172.

PTM databases

iPTMnetiP35172.

Interactioni

Protein-protein interaction databases

BioGridi32702. 35 interactions.
DIPiDIP-6841N.
IntActiP35172. 3 interactions.
MINTiMINT-665495.

Structurei

3D structure databases

ProteinModelPortaliP35172.
SMRiP35172. Positions 324-739.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni338 – 3392Substrate bindingBy similarity
Regioni384 – 3863Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006949.
HOGENOMiHOG000192885.
InParanoidiP35172.
KOiK01194.
OMAiLTHKVQV.
OrthoDBiEOG751NPZ.

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. 3 hits.
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.

P35172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDFLPKVTE INPPSEGNDG EDNIKPLSSG SEQRPLKEEG QQGGRRHHRR
60 70 80 90 100
LSSMHEYFDP FSNAEVYYGP ITDPRKQSKI HRLNRTRTMS VFNKVSDFKN
110 120 130 140 150
GMKDYTLKRR GSEDDSFLSS QGNRRFYIDN VDLALDELLA SEDTDKNHQI
160 170 180 190 200
TIEDTGPKVI KVGTANSNGF KHVNVRGTYM LSNLLQELTI AKSFGRHQIF
210 220 230 240 250
LDEARINENP VDRLSRLITT QFWTSLTRRV DLYNIAEIAR DSKIDTPGAK
260 270 280 290 300
NPRIYVPYNC PEQYEFYIQA SQMNPSLKLE VEYLPKDITA EYVKSLNDTP
310 320 330 340 350
GLLALAMEEH VNPSTGERSL VGYPYAVPGG RFNELYGWDS YLMALGLIES
360 370 380 390 400
NKVDVARGMV EHFIFEIDHY SKILNANRSY YLCRSQPPFL TDMALLVFEK
410 420 430 440 450
IGGKNNPNAI QLLKRAFRAA IKEYKEVWMS SPRLDSLTGL SCYHSDGIGI
460 470 480 490 500
PPETEPDHFD TILLPYAEKY NVTLEKLRYL YNEGMIKEPK LDAFFLHDRA
510 520 530 540 550
VRESGHDTTY RFEGVCAYLA TIDLNSLLYK YEKDIAFVIK EYFGNEYKDE
560 570 580 590 600
NDGTVTDSEH WEELAELRKT RINKYMWDED SGFFFYYNTK LKCRTSYESA
610 620 630 640 650
TTFWSLWAGL ATEEQAKITV EKALPQLEML GGLVACTEKS RGPISIDRPI
660 670 680 690 700
RQWDYPFGWA PHQILAWKGL SAYGYQQVAT RLAYRWLYMI TKSFVDYNGM
710 720 730 740 750
VVEKYDVTRG TDPHRVDAEY GNQGADFKGV ATEGFGWVNT SYLLGLKYMN
760 770 780
NHARRALAAC SPPLPFFNSL KPSEKKLYYL
Length:780
Mass (Da):89,679
Last modified:February 1, 1994 - v1
Checksum:iB034B14A68B38C53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26494 Genomic DNA. Translation: CAA81270.1.
Z35870 Genomic DNA. Translation: CAA84937.1.
BK006936 Genomic DNA. Translation: DAA07122.1.
PIRiS44560.
RefSeqiNP_009555.1. NM_001178349.1.

Genome annotation databases

EnsemblFungiiYBR001C; YBR001C; YBR001C.
GeneIDi852286.
KEGGisce:YBR001C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26494 Genomic DNA. Translation: CAA81270.1.
Z35870 Genomic DNA. Translation: CAA84937.1.
BK006936 Genomic DNA. Translation: DAA07122.1.
PIRiS44560.
RefSeqiNP_009555.1. NM_001178349.1.

3D structure databases

ProteinModelPortaliP35172.
SMRiP35172. Positions 324-739.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32702. 35 interactions.
DIPiDIP-6841N.
IntActiP35172. 3 interactions.
MINTiMINT-665495.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

PTM databases

iPTMnetiP35172.

Proteomic databases

MaxQBiP35172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR001C; YBR001C; YBR001C.
GeneIDi852286.
KEGGisce:YBR001C.

Organism-specific databases

EuPathDBiFungiDB:YBR001C.
SGDiS000000205. NTH2.

Phylogenomic databases

GeneTreeiENSGT00390000006949.
HOGENOMiHOG000192885.
InParanoidiP35172.
KOiK01194.
OMAiLTHKVQV.
OrthoDBiEOG751NPZ.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17147.
YEAST:YBR001C-MONOMER.

Miscellaneous databases

NextBioi970922.
PROiP35172.

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. 3 hits.
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. "Sequence around the centromere of Saccharomyces cerevisiae chromosome II: similarity of CEN2 to CEN4."
    Wolfe K.H., Lohan A.J.E.
    Yeast 10:S41-S46(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae."
    Nwaka S., Kopp M., Holzer H.
    J. Biol. Chem. 270:10193-10198(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTREB_YEAST
AccessioniPrimary (citable) accession number: P35172
Secondary accession number(s): D6VQ02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.