ID A0A0A2VR60_BEABA Unreviewed; 961 AA.
AC A0A0A2VR60;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE AltName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=BBAD15_g5812 {ECO:0000313|EMBL:KGQ08842.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08842.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ08842.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08842.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000256|ARBA:ARBA00004833}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
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:KGQ08842.1}.
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DR EMBL; ANFO01000533; KGQ08842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VR60; -.
DR STRING; 1245745.A0A0A2VR60; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0017177; C:glucosidase II complex; IEA:EnsemblFungi.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0106407; F:Glc2Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006491; P:N-glycan processing; IEA:EnsemblFungi.
DR CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
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 PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
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.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..961
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002007154"
FT DOMAIN 94..329
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 386..714
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 722..811
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 833..872
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 209..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..225
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 109280 MW; 25806F179FEB158F CRC64;
MALRSQWIAL LIALGILMCL VMPGASVKEH DFKKCDQSGF CKRNRAYADK ATTEGSRWQS
PYTVQPSSVS FKDGQLHAVI HKTINANGDT VNLPITVSFL KSGNARVTVD EERRQKQDIE
LRHDSKVRKE RYNEAEKWVL VGGLALDKDA KVSHQDDAQT NVQYGKEGNL EAAIKYSPLA
IDFRRDGVSH VRFNDRGLLN VEHWRPKIER EEGQEEKDSE DESTWWDETF GGNTDSKPRG
PESIALDISF LGYEHVFGIP EHTGSLSLKQ TRGGSGNHNE PYRMYNSDVF EYILDSPMTL
YGSIPFMQAH KKDSTVGVFW LNAAETWVDI VKSKAATNPL TLGKTGKTNT ETHWISESGL
IDVFVFLGPT PQDVTRTYGE LTGYSAMPQE FAIGYHQCRW NYISDDDVKD VDRKMDKYKI
PYDVIWLDIE YLDDRKYFTW DPHSFADPTG MGKQLDDHSR QLVIIIDPHI KKLEGYSIYD
ELSSQDLAVY DKEGKPYEGW CWPGSSNWVD CFNPKAIEWW KTLYKYDKFA GTAENTFIWN
DMNEPSVFNG PETTMPKDNI HFGQWEHRDI HNINGLTFHN ATFEALKTRK KGELRRPFVL
TRSFYSGSQR LGAMWTGDNQ ATWEHLAASI PMVLNQGISG FPFAGADVGG FFGNPSKDLM
ARWYQAGAFY PFYRGHAHID SRRREPYLLG EPYTGILTQA LRLRYALLPS WYTAFFQANR
DGSPIVRPMY WTHPSEEAGF AIDDQLFVGS TGILVKPIVE ENKFSTDIWI PDEEVYYDYT
TYDVVNTQKA KRVTIAAAID QIPMLMRGGH VFARRDIPRR SALAMKYDDY TLVVSVSRDG
TATGELYADD GDTFEHEKGQ YIYRKFSFDK DGVRSVDAEG RSAKSVKAGA WLKEQSRVHI
DKIVIVGATD AWNRKEVEIE SDGKTWTVPV DYHEAAKGRA AYAVVGRVGA KISSDWSIKL
A
//