ID Q6BRR1_DEBHA Unreviewed; 1100 AA.
AC Q6BRR1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN OrderedLocusNames=DEHA2D14498g {ECO:0000313|EMBL:CAG87277.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG87277.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG87277.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000256|ARBA:ARBA00001576};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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DR EMBL; CR382136; CAG87277.2; -; Genomic_DNA.
DR RefSeq; XP_459109.2; XM_459109.1.
DR AlphaFoldDB; Q6BRR1; -.
DR STRING; 284592.Q6BRR1; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR GeneID; 2900907; -.
DR KEGG; dha:DEHA2D14498g; -.
DR VEuPathDB; FungiDB:DEHA2D14498g; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; Q6BRR1; -.
DR OMA; ANHVDAG; -.
DR OrthoDB; 1769273at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..394
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 456..667
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
SQ SEQUENCE 1100 AA; 122137 MW; 2852E893D48FE862 CRC64;
MEYDSIGERF KHRTISKIDY CNIFIHKFCK RQIVIKTMVV LNFILIFVLY SYYHGITYAL
PFTIKDIDID DSFNDSTVSF ETIENNKKQL ESLINSRENK EIFLQLQNSG SAYYDPTSNT
VGTAEFPTYN QYQRQAYVSN GYIGSRIPNL GQGFTFDQLS DSPDAVEDDL SNGWPLFNER
FSGSFIGGFY DIQKNTTETN FPELIEKGYE SILSAVPQWT TLTLSTVKNG KTLSLDPSLS
RDSQGDISNY AQNLSLSNGI VTTEFTWLES IQVHFEVVAH RSNINLGIVN LRIVNLDNST
VDLKVEDKLD FASTQRCQLS EVGSDEEGIF IHFQPNEIDY VNGAIYSTLQ YDEMSSNAIS
RGSTNDTSTQ KLDISVEPSK SFKISKLVGI VSSDLDPEKY KSHNTVNDFA KEVATKQKDS
VSKLIKSHKV GWARTFESSN SITFSGDPLL TLASRASIYH LNANTRPGAQ GVTAALPVGG
LSSDSYGGMV FWDTDLWMLN GLLPFNPDHA KSIVNYRIHT HEQAIKNVPN NESGAVYSWT
SGRFGNCTST GPCLDYEYHI NVAVAMAAWE VYLSGAADDD YLDSVAYPLI NDAATFLADY
VKYNESLAQY VSHNMTDPDE YANHVDNAAY TNAGISLLMK WAITISNHLG KPVPSKYTDI
AGSMHIPTSD NHDNITLEYT GMNSSVGIKQ ADVIMMTYPL GNELISDDQA YTNMEFYSMK
QVSYGPAMTF PIFSIVASNL SPSGCASQSY LHKAVQPFLR GPFAQFSEQN NDNFLTNGGT
HPAFPFMTAH GGFLQAILQG LTGLRFDFDL DDRNKLSRML TLDPISLPCL GNGVQFDSIK
YMNQSISLAI NETSFIIKHN GPIAGGDSDS IRISLAKRNP KSGVYTLDKG EELVFPLFVP
TAGSQLSVSE CASAKFINIT ESAYGDATVS VNDGDNTTHW QSKYNDTTAK ILVDLKQSRN
LTSGAINWGD RPPKSWSLSA FGSEEQSKIN DLNDVIDFLS KVNFGNDLYK KYQFIDAGTI
YDQDDVFTTI VSEEVDISAP FDPKDYAEVK IPSRHNTTSF NIEQGLGARF LLIEVTDIHD
TEPIDDETGG AKLYEVEFFE
//
