ID A0A1D2VAS3_9ASCO Unreviewed; 1104 AA.
AC A0A1D2VAS3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=alpha,alpha-trehalase {ECO:0000256|ARBA:ARBA00012757};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757};
GN ORFNames=ASCRUDRAFT_38546 {ECO:0000313|EMBL:ODV58776.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV58776.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV454489; ODV58776.1; -; Genomic_DNA.
DR RefSeq; XP_020045083.1; XM_020190868.1.
DR AlphaFoldDB; A0A1D2VAS3; -.
DR STRING; 1344418.A0A1D2VAS3; -.
DR GeneID; 30964504; -.
DR InParanoid; A0A1D2VAS3; -.
DR OrthoDB; 1769273at2759; -.
DR Proteomes; UP000095038; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ODV58776.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..415
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 473..701
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT COILED 422..449
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1104 AA; 125989 MW; FAAA97C652045402 CRC64;
MNIKGPLLIN FHERKIYNRK SFKIFILLIF TFLGIFYLIY STLFSIFPSQ NHHSYLPFFF
HPFSSNHHGT FHGKREFIKQ KILAKFYNKY CNKNYESYVA KKDYLEKSKE IFKLCSNSKN
SFYNDDDDKN YLGTTVFSEN IFNKQPYISN GYIGSRLTNL GQGFAFDQSS PGNYQYEQNP
DSFSNGWPLF NKRFSGAFIA GFYNLQYRTP GVNFPELLDI GYESVLSAIP QFTTLNIKYN
DLILNPELTK PNEISNYSQI MSLNNAIVQT SFIWQDALKV SFETFAHRSI STLALVSLNI
TNLIHNETHL EIIDNLNFNT SQRCDLEELG YKKKENSIYM VVTPNNLPYS FASIYSSWDY
QHTIDITNQK HTKLKKPKVN YSIQNNQSVN KVLYINLKPY ESLSLNKYVG IVSSDYEKLD
ISSDYESLLK STKEQLNQIK KKVESHIDSW NKVLNGIKIE VPSDGLLTLS ARSSLFHLLV
NTREDSKGVT SALPVSGLSS DSYGGMVFWD TDIWMIPGLL PFAPEHAKAL TYYRYFTFEQ
AKRNAKYYDS PGSVYPWTSG RFGNCTATGP CVDYEYHINI AISLSMWKVF LSGAGDLNYL
EEVAWPIIKN SANFLSAYVK YNETLKQYTT FNLTDPDEYA DFIDNGAYTN AGISTLMKWA
LLIASESLLN KTEEINPKWL SIVGNMYIPK SEYNITLEYD GMNSSVLIKQ ADVVLSTYPL
EDFDIDIEQG LRDMHYYTEK QADAGPAMTF PVFSIISSRL SKKGCSSQSF LKKSSYPYIR
LPFGQFSEQS NDDYLINGGT QPAFPFLTAN GGLIQAITYG LPGIRFGYII NPNGDFQRVL
KFDPISLPIL PEGVIIKGFK YLGQLLDIII TNEEAIILHN GDLDSNIENG DTILIEVEER
NFNKGLYELN SGDEFIVPLF FPEKNINGSI SECFPILNLS DGKYGDVANS ANDGDNSTSW
QPINDQEAKL IIDLENYLQI HKVIINWGNR PAEYLNVSII DGEINEEIDE IQREFKGKKE
NEFEEILVEI SRNDKLIIEN CKINISHPYD AEEFGKVQLM PDNITEINIE EMSIRSRFII
VGVKGNLNGD YDRRGCTIAE ISII
//
