ID H0EW41_GLAL7 Unreviewed; 924 AA.
AC H0EW41;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative alpha/beta-glucosidase agdC {ECO:0000313|EMBL:EHK97248.1};
GN ORFNames=M7I_6978 {ECO:0000313|EMBL:EHK97248.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97248.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK97248.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Has both alpha- and beta-glucosidase activity.
CC {ECO:0000256|ARBA:ARBA00025512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001657};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK97248.1}.
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DR EMBL; AGUE01000200; EHK97248.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EW41; -.
DR HOGENOM; CLU_000631_11_0_1; -.
DR InParanoid; H0EW41; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF67; ALPHA_BETA-GLUCOSIDASE AGDC-RELATED; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..924
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003532826"
FT DOMAIN 106..224
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 272..666
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 668..700
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 708..796
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 445..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 103582 MW; 467C6C69CCCEEB0E CRC64;
MLQKFVTGLA WASTVSGAAL SRRQATSDSC PGYSASGVVQ TATGLTADLT LAGAACNVYG
NDIQNLKLTV NYDSDSRLHV KIEDAANIAY RVPQSVFPTP DSNASVSAAD SALEFSHVDS
PFSFKVTRKS SGEVLFDTSA ASLIFEDQYL RVRTSLPENP NIYGLGEHSD SLRLNTTDYT
RTLWSRDSYG IPAGTNLYGN HPIYFDHRGS SGTHGVFLLS SSGMDVKINR TQTDGQYLEY
NLMSGILDFY FIDGPSPKQV AEHYSEVSGK AAMMPYWGFG FHQCRYGYRD YFAIAEVIAN
YSKADIPLET MWTDIDYMYE RYIMTTDPDR FPIARVREYV DYLHAHNQHY IVMVDPAMAF
QTKRENDLPY QTFLRAQEQG ILLQKNGADY QGVVWPGVTA FPDWFHPDTQ SYWNNEFLEF
FNAETGMDID ALWIDMNEAA NFNYFGDNPQ DSAEERGFPP RRPALRSQPR PIPGFPQAFQ
PDPNSPYAPD DYSYAPPWLA PPATPNEKRS SKRTPLEANM LENRQASQVI GYPNRNLLAP
PYQINNENTV EAYGGLSNFT LDTDIIHYDG HVELDVHNIY GAQMSEFSRN ALEARRPGRR
PMVITRSTFA GSGKAVGKWL GDNLSTWELY RQSIQGMLDF AAIYQMPMVG SDVCGFGANT
TETLCASSIP QEFYLWDTVA EAARKTMSIR YRLLDYIYTA LYKQSTIGTP LINPMFFTYP
EDEKTFAVEL QFFYGEHILV SPVTEENSTS VDIYLPNDLF YDFYTYAPVQ GTGAMLTLND
IDFTSIPLHI KSGAVIPMRN VRTKPFSFIV APTAAGEAAG ELYLDDGDSI VQHETSEIKM
TYHEKMLTID GNFSYQAGCD SLQDVTILGV HTAPTGAYWS KGSDAHEVVW YTCPAGGWKH
DAEKESLTIT IETKLDAPIK VKYE
//
