ATH1_CANGB
ID ATH1_CANGB Reviewed; 1212 AA.
AC M1RNJ8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Periplasmic/secreted acid trehalase ATH1 {ECO:0000305};
DE Short=cgATH1 {ECO:0000303|PubMed:26411890};
DE EC=3.2.1.28 {ECO:0000305|PubMed:26411890, ECO:0000305|PubMed:33146242};
GN Name=ATH1 {ECO:0000303|PubMed:26411890};
OS Candida glabrata (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=5478 {ECO:0000312|EMBL:AGG12634.1};
RN [1] {ECO:0000312|EMBL:AGG12634.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Bg14 {ECO:0000312|EMBL:AGG12634.1};
RX PubMed=26411890; DOI=10.1016/j.micres.2015.06.008;
RA Zilli D.M., Lopes R.G., Alves S.L. Jr., Barros L.M., Miletti L.C.,
RA Stambuk B.U.;
RT "Secretion of the acid trehalase encoded by the CgATH1 gene allows
RT trehalose fermentation by Candida glabrata.";
RL Microbiol. Res. 179:12-19(2015).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bg14 {ECO:0000303|PubMed:33146242};
RX PubMed=33146242; DOI=10.1590/0074-02760200401;
RA Lopes R.G., Munoz J.E., Barros L.M., Alves-Jr S.L., Taborda C.P.,
RA Stambuk B.U.;
RT "The secreted acid trehalase encoded by the CgATH1 gene is involved in
RT Candida glabrata virulence.";
RL Mem. Inst. Oswaldo Cruz 115:e200401-e200401(2020).
CC -!- FUNCTION: Periplasmic/secreted acid trehalase that catalyzes hydrolysis
CC of the disaccharide trehalose and required for growth on trehalose as
CC carbon source (PubMed:26411890, PubMed:33146242). Growth on trehalose
CC is not restricted to respiration (PubMed:26411890).
CC {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:33146242}.
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:26411890, ECO:0000305|PubMed:33146242};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26411890}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26411890,
CC ECO:0000269|PubMed:33146242}. Periplasm {ECO:0000269|PubMed:26411890,
CC ECO:0000269|PubMed:33146242}. Membrane {ECO:0000250|UniProtKB:P48016};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P48016}.
CC -!- DISRUPTION PHENOTYPE: Abolishes growth in trehalose carbon source
CC (PubMed:33146242). Normal growth in glucose carbon source
CC (PubMed:33146242). Decreases virulence in a mouse infection model
CC (PubMed:33146242). {ECO:0000269|PubMed:33146242}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; KC208027; AGG12634.1; -; Genomic_DNA.
DR AlphaFoldDB; M1RNJ8; -.
DR SMR; M1RNJ8; -.
DR VEuPathDB; FungiDB:CAGL0K05137g; -.
DR VEuPathDB; FungiDB:GWK60_K04983; -.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IDA:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; IDA: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; Glycosidase; Hydrolase; Membrane; Periplasm; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1212
FT /note="Periplasmic/secreted acid trehalase ATH1"
FT /id="PRO_0000452329"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..1212
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 677
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 546..547
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 744..745
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1212 AA; 136519 MW; 2DB70E1AB18662C9 CRC64;
MGFKDKILFW KDEVQYRTLA VADQVANRFL HSFENVYQGD ESVEDADSRP VGLTNETLSH
SSDFFVLPEE RISTRVKIRR QNILNTTLIL GMLIALVIWT AILSTNSYFS SSLASASPLF
NKEGRVVRPM RESNLGLHAD PQTRKSSKTL YDLLSDFDNA FYDDENMILG SLAFGENTYS
RQPYVANGYI GSRIPNIGFG YALDTLNLYA DAPGALNNGW PLRNRRFAGS FVSDFYSLQA
KLNSTNFPEL DEKGYTTVIS SIPEWTDLQF TVDLNGTKWF NPQSVLIDDV INYNQNLSMK
DGIVSTNMDW LNGMINIKSE VWAHRKIHSL GITRLEISLN LDALPDEFTE LPVTVYDIID
LNTSHRTTLY EKGQDEDNKA IYMIVNPDNV PYSNAVVYST CTIKGTENNF SPYNFTSDDR
IARNYMTNLT EENPKVVIYK YTSVVSSEYN NDEPNPNVNL KFASNIANTA KGNYKSLLSN
HKRAWYDLYN DAFIEIPSDS LLEMTARSSL FHLLANTRQY NVSTTRGLPV GVGGLSSDSY
GGMVFWDADV WMAPALLPFF PNIAMNMNNY RNATHQQAIE NAKQYNYPGA VYPWTSGRYA
NCTSTGPCID YEYHINVDIA LASFSIYMNG AEGADEDYLR FTTWPMVKDA AVFFKAYVKY
NETLGEYETY NLTDPDEFAN HVNNGAFTNA GIKTLLKWAT DIGTHLGEEV DPKWMEIADN
IHIPRSDSNI TLEYSGMNSS VEIKQADVTL MVYPLGYIND ESILNNAIKD LYYYSERQSA
SGPAMTYPVF VAAAASLLNH GSSSQSYLYK SVLPYLRSPF AQFSEQSDDN FLTNGLTQPA
FPFLTANGGF LQSILFGLTG LRYSYEVTPR TKKISRLLKF DPVKLPLLPG GIAIRNFKYM
GQVLDIIIDD NNGTIAHKGG DKPIRIKVPN RDILHDRNIT SALYSKRDDD LSATDDYYGT
YFTLYPNEEL VIPLYDTKLN IDGNIAESKQ ITNLTAGVPG DVGFSALDGN NYTHWQPFDK
SDNAKLLIDL GFNSTHVIKK GIILWGQRPA KNISLSVLPH SERIEQLFAN ITDLLETSSI
TKGGLPLNQM LGQTQSNVTA EIDDDILALL NWKGDDLDQL IPYLPDMHLL QEKFIPILKD
YPIKPNQRYY EEIIDDDIIK LLPSNTTEFT IDYNSIPGGE KRARYVVLTV HGTYDDDDDL
KGATIREIVL QE
