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Protein

Neutral trehalase

Gene

NTH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Activated by cAMP-dependent phosphorylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei302 – 3021SubstrateBy similarity
Binding sitei346 – 3461SubstrateBy similarity
Binding sitei355 – 3551SubstrateBy similarity
Binding sitei476 – 4761Substrate; via carbonyl oxygenBy similarity
Active sitei478 – 4781Proton donor/acceptorBy similarity
Active sitei674 – 6741Proton donor/acceptorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to desiccation Source: SGD
  • trehalose catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17146.
YEAST:YDR001C-MONOMER.

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:NTH1
Synonyms:NTH
Ordered Locus Names:YDR001C
ORF Names:YD8119.07C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR001C.
SGDiS000002408. NTH1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 751750Neutral trehalasePRO_0000173798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei58 – 581PhosphothreonineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32356.

PTM databases

iPTMnetiP32356.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
BMH1P293116EBI-19509,EBI-3661
BMH2P347308EBI-19509,EBI-3672

Protein-protein interaction databases

BioGridi32054. 59 interactions.
DIPiDIP-1479N.
IntActiP32356. 16 interactions.
MINTiMINT-392566.

Structurei

3D structure databases

ProteinModelPortaliP32356.
SMRiP32356. Positions 295-711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni309 – 3102Substrate bindingBy similarity
Regioni355 – 3573Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006949.
HOGENOMiHOG000192885.
InParanoidiP32356.
KOiK01194.
OMAiMNSHARR.
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.

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

P32356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVNTSQGP VAQGRQRRLS SLSEFNDPFS NAEVYYGPPT DPRKQKQAKP
60 70 80 90 100
AKINRTRTMS VFDNVSPFKK TGFGKLQQTR RGSEDDTYSS SQGNRRFFIE
110 120 130 140 150
DVDKTLNELL AAEDTDKNYQ ITIEDTGPKV LKVGTANSYG YKHINIRGTY
160 170 180 190 200
MLSNLLQELT IAKSFGRHQI FLDEARINEN PVNRLSRLIN TQFWNSLTRR
210 220 230 240 250
VDLNNVGEIA KDTKIDTPGA KNPRIYVPYD CPEQYEFYVQ ASQMHPSLKL
260 270 280 290 300
EVEYLPKKIT AEYVKSVNDT PGLLALAMEE HFNPSTGEKT LIGYPYAVPG
310 320 330 340 350
GRFNELYGWD SYMMALGLLE ANKTDVARGM VEHFIFEINH YGKILNANRS
360 370 380 390 400
YYLCRSQPPF LTEMALVVFK KLGGRSNPDA VDLLKRAFQA SIKEYKTVWT
410 420 430 440 450
ASPRLDPETG LSRYHPNGLG IPPETESDHF DTVLLPYASK HGVTLDEFKQ
460 470 480 490 500
LYNDGKIKEP KLDEFFLHDR GVRESGHDTT YRFEGVCAYL ATIDLNSLLY
510 520 530 540 550
KYEIDIADFI KEFCDDKYED PLDHSITTSA MWKEMAKIRQ EKITKYMWDD
560 570 580 590 600
ESGFFFDYNT KIKHRTSYES ATTFWALWAG LATKEQAQKM VEKALPKLEM
610 620 630 640 650
LGGLAACTER SRGPISISRP IRQWDYPFGW APHQILAWEG LRSYGYLTVT
660 670 680 690 700
NRLAYRWLFM MTKAFVDYNG IVVEKYDVTR GTDPHRVEAE YGNQGADFKG
710 720 730 740 750
AATEGFGWVN ASYILGLKYM NSHARRALGA CIPPISFFSS LRPQERNLYG

L
Length:751
Mass (Da):85,879
Last modified:October 1, 1996 - v3
Checksum:iE6687F2E9377E49F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti514 – 5152CD → NN in AAA66896 (PubMed:3537685).Curated
Sequence conflicti712 – 7121S → R in CAA46718 (PubMed:8444853).Curated
Sequence conflicti712 – 7121S → R in AAA66896 (PubMed:3537685).Curated
Sequence conflicti723 – 7242HA → YE in CAA46718 (PubMed:8444853).Curated
Sequence conflicti723 – 7242HA → YE in AAA66896 (PubMed:3537685).Curated
Sequence conflicti727 – 7282AL → EI in CAA46718 (PubMed:8444853).Curated
Sequence conflicti727 – 7282AL → EI in AAA66896 (PubMed:3537685).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65925 Genomic DNA. Translation: CAA46718.1.
Z48008 Genomic DNA. Translation: CAA88061.1.
M13000 Genomic DNA. Translation: AAA66896.1.
BK006938 Genomic DNA. Translation: DAA11848.1.
PIRiS50982.
RefSeqiNP_010284.1. NM_001180309.1.

Genome annotation databases

EnsemblFungiiYDR001C; YDR001C; YDR001C.
GeneIDi851564.
KEGGisce:YDR001C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65925 Genomic DNA. Translation: CAA46718.1.
Z48008 Genomic DNA. Translation: CAA88061.1.
M13000 Genomic DNA. Translation: AAA66896.1.
BK006938 Genomic DNA. Translation: DAA11848.1.
PIRiS50982.
RefSeqiNP_010284.1. NM_001180309.1.

3D structure databases

ProteinModelPortaliP32356.
SMRiP32356. Positions 295-711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32054. 59 interactions.
DIPiDIP-1479N.
IntActiP32356. 16 interactions.
MINTiMINT-392566.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

PTM databases

iPTMnetiP32356.

Proteomic databases

MaxQBiP32356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR001C; YDR001C; YDR001C.
GeneIDi851564.
KEGGisce:YDR001C.

Organism-specific databases

EuPathDBiFungiDB:YDR001C.
SGDiS000002408. NTH1.

Phylogenomic databases

GeneTreeiENSGT00390000006949.
HOGENOMiHOG000192885.
InParanoidiP32356.
KOiK01194.
OMAiMNSHARR.
OrthoDBiEOG751NPZ.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17146.
YEAST:YDR001C-MONOMER.

Miscellaneous databases

PROiP32356.

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. "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae."
    Kopp M., Mueller H., Holzer H.
    J. Biol. Chem. 268:4766-4774(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Corrected sequence of the yeast neutral trehalase-encoding gene (NTH1): biological implications."
    Kopp M., Nwaka S., Holzer H.
    Gene 150:403-404(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Structure and sequence of the centromeric DNA of chromosome 4 in Saccharomyces cerevisiae."
    Mann C., Davis R.W.
    Mol. Cell. Biol. 6:241-245(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-751.
    Strain: ATCC 204508 / S288c.
  6. "Purification and characterization of neutral trehalase from the yeast ABYS1 mutant."
    App H., Holzer H.
    J. Biol. Chem. 264:17583-17588(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-58; SER-60; SER-66 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-66 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-20; SER-21; SER-23; THR-58; SER-60; SER-66 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTREA_YEAST
AccessioniPrimary (citable) accession number: P32356
Secondary accession number(s): D6VRY8, E9P9U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1840 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.