ID   ATH1_YEASC              Reviewed;        1211 AA.
AC   N1P212;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Periplasmic acid trehalase ATC1 {ECO:0000303|PubMed:15128531};
DE            EC=3.2.1.28 {ECO:0000305|PubMed:15128531};
GN   ORFNames=CENPK1137D_1727 {ECO:0000312|EMBL:EIW07140.1};
OS   Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=889517 {ECO:0000312|Proteomes:UP000013192};
RN   [1] {ECO:0000312|Proteomes:UP000013192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEN.PK113-7D {ECO:0000312|Proteomes:UP000013192};
RX   PubMed=22448915; DOI=10.1186/1475-2859-11-36;
RA   Nijkamp J.F., van den Broek M., Datema E., de Kok S., Bosman L.,
RA   Luttik M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA   Klaassen P., Paddon C.J., Platt D., Koetter P., van Ham R.C.,
RA   Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT   "De novo sequencing, assembly and analysis of the genome of the laboratory
RT   strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT   biotechnology.";
RL   Microb. Cell Fact. 11:36-36(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15128531; DOI=10.1128/aem.70.5.2771-2778.2004;
RA   Jules M., Guillou V., Francois J., Parrou J.L.;
RT   "Two distinct pathways for trehalose assimilation in the yeast
RT   Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 70:2771-2778(2004).
CC   -!- FUNCTION: Periplasmic acid trehalase that catalyzes hydrolysis of the
CC       disaccharide trehalose and required for growth on trehalose as carbon
CC       source (PubMed:15128531). Growth on trehalose is strictly respiratory
CC       (PubMed:15128531). {ECO:0000269|PubMed:15128531}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000305|PubMed:15128531};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P48016}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:P48016}. Vacuole
CC       lumen {ECO:0000250|UniProtKB:P48016}. Periplasm
CC       {ECO:0000269|PubMed:15128531}. Note=May localize to the periplasm
CC       either as a membrane-bound or as a free protein (PubMed:15128531).
CC       Vacuolar localization appears to be associated with its degradation (By
CC       similarity). {ECO:0000250|UniProtKB:P48016,
CC       ECO:0000269|PubMed:15128531}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P48016}.
CC   -!- DISRUPTION PHENOTYPE: Severely decreases growth on trehalose carbon
CC       source, simultaneous disruption of AGT1 or NTH1 abolishes growth.
CC       {ECO:0000269|PubMed:15128531}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; CM001537; EIW07140.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1P212; -.
DR   SMR; N1P212; -.
DR   EnsemblFungi; EIW07140; EIW07140; CENPK1137D_1727.
DR   HOGENOM; CLU_006285_4_0_1; -.
DR   Proteomes; UP000013192; Chromosome XVI.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IMP:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IMP:UniProtKB.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Membrane; Periplasm; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..1211
FT                   /note="Periplasmic acid trehalase ATC1"
FT                   /id="PRO_0000452330"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..1211
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          70..131
FT                   /note="Required for cell surface targeting"
FT                   /evidence="ECO:0000250|UniProtKB:P48016"
FT   ACT_SITE        644
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         513..514
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         711..712
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        638
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        696
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        705
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        879
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        897
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        910
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        972
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        990
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1031
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1049
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1064
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1211 AA;  136921 MW;  34AEC44B0B648DEC CRC64;
     MKRIRSLWFN AEASYSNLNN SPSLRNKNST GNNSRSKNYR SFSRFDLINS ILLLMMLFLL
     AIFVTALYLT KSSRLTYSHA SRAALFNPLG VISPSLGNHT LNYDPEARES SKKLYELLSD
     FNTAYYDDEN MILGSNLFSK NTYSRQPYVA NGYIGSRIPN IGFGYALDTL NFYTDAPGAL
     NNGWPLRNHR FAGAFVSDFY CLQPKLNSTN FPELDDVGYS TVISSIPQWT NLQFSLVNDS
     KWFNPQNVTL DDVTNYSQNL SMKDGIVTTE LDWLNSQIHV KSEIWAHRHI HPLGVVSLEI
     SLNTDHLPSD FDSLDVNIWD ILDFNTSHRT VLHSTGTDEK NNAVFMIVQP DNVPSSNCAI
     YSTCTVKYEN STNPINSSES FEEKDVSSNI YNVILTEDQP KIIVHKYVGI MSTEFNKNKE
     QQDNTNIGLA KMIALNSKGN YEKLLSSHKR AWYDLYNDAF IEIPSDSLLE MTARSSLFHL
     LANTRDYNVS SDRGLPVGVS GLSSDSYGGM VFWDADIWME PALLPFFPNV AQNMNNYRNA
     THSQAKLNAE KYGYPGAIYP WTSGKYANCT STGPCVDYEY HINVDVAMAS FSIYLNGHEG
     IDDEYLRYTT WPIIKNAAQF FTAYVKYNSS LGLYETYNLT DPDEFANHIN NGAFTNAGIK
     TLLKWATDIG NHLGEVVDPK WSEISKDIYI PRSSSNITLE YSGMNSSVEI KQADVTLMVY
     PLGYINDESI LNNAIKDLYY YSERQSASGP AMTYPVFVAA AAGLLNHGSS SQSYLYKSVL
     PYLRAPFAQF SEQSDDNFLT NGLTQPAFPF LTANGGFLQS ILFGLTGIRY SYEVDPDTKK
     INRLLRFNPI ELPLLPGGIA IRNFKYMNQV LDIIIDDHNG TIVHKSGDVP IHIKIPNRSL
     IHDQDINFYN GSENERKPNL ERRDVDRVGD PMRMDRYGTY YLLKPKQELT VQLFKPGLNA
     RNNIAENKQI TNLTAGVPGD VAFSALDGNN YTHWQPLDKI HRAKLLIDLG EYNEKEITKG
     MILWGQRPAK NISISILPHS EKVENLFANV TEIMQNSGND QLLNETIGQL LDNAGIPVEN
     VIDFDGIEQE DDESLDDVQA LLHWKKEDLA KLIEQIPRLN FLKRKFVKIL DNVPVSPSEP
     YYEASRNQSL IEILPSNRTT FTIDYDKLQV GDKGNTDWRK TRYIVVAVQG VYDDYDDDNK
     GATIKEIVLN D