ID A0A395HN04_ASPHC Unreviewed; 963 AA.
AC A0A395HN04;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
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=BO97DRAFT_396768 {ECO:0000313|EMBL:RAL09140.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09140.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL09140.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09140.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824306; RAL09140.1; -; Genomic_DNA.
DR RefSeq; XP_025548294.1; XM_025694101.1.
DR AlphaFoldDB; A0A395HN04; -.
DR STRING; 1450537.A0A395HN04; -.
DR GeneID; 37198390; -.
DR VEuPathDB; FungiDB:BO97DRAFT_396768; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0017177; C:glucosidase II complex; IEA:TreeGrafter.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IEA:TreeGrafter.
DR CDD; cd06603; GH31_GANC_GANAB_alpha; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..963
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017210909"
FT DOMAIN 97..333
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 390..718
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 726..815
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 834..878
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 212..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 109756 MW; 66F0F730E00656F3 CRC64;
MAGFRPLSTR WTLLFSLVIL LGCLVIPGVT VKHESFKTCS QSGFCKRNRA FADEVTAKGS
SWSSPYELES SSIQFKDGQL HGTVLKTLSA NEKIRLPLVI SFLESGVARV TVDEEKRMKG
EIELRHNSQA RKERYNEVEK WALVGNLELS KTATLEPETE AGATRVLYGP DNKFEAIIHH
APFRAEFKRD GETHVQLNHQ GYLNWEHWRP KTETAEDSDQ QPSEDESTWW DESFGGNTDS
KPRGPESVGL DITFPGYSHV FGIPEHADSM SLKQTRGGDG NHAEPYRMYN SDVFEYELNS
PMTLYGSIPF MQAHRKDSTV GVFWLNAAET WVDIVKSTSS PNPLSLGVGA KTDTQSHWFS
ESGQIDVFVF LGPTPQDISK TYGELTGFTQ LPQHFAIAYH QCRWNYITDE DVKEVDRNFD
KYQIPYDIIW LDLEYTDDRK YFTWDPLTFP DPISMEKQLD ASERKLVVLI DPHIKNKEGF
TVSEELKSKD LATKNKDGEI YDGWCWPGSS NWIDTFNPAA IKWWVSLFKY DRFKGTLSNV
FIWNDMNEPS VFNGPETTMP KDNIHHGNWE HRDIHNVHGI TLVNATYEAL LERKKGEVRR
PFILTRSYYA GAQRMSAMWT GDNQATWEHL AASLPMVLNN GIAGFPFAGA DVGGFFQNPS
KELLTRWYQT GIWYPFFRAH AHIDTRRREP YLIAEPFRST IAQAIRLRYQ LLPAWYTAFH
EASVNGMPIV RPQYYVHPAD EAGFAIDDQL YLGNTGLLAK PVVSEDVTSV DIYLADDEKY
YDYFDYTVYH GAGKRHTVPA PMEKIPLLMQ GGHVIPRKDR PRRSSGLMRW DPYTLVIVLD
KNGQADGTLY VDDGETFDYE RGAYIHRRFA YRDSALSSED LGIKGPKTND YLKAMAGVRV
ERVIVVDPPK DWQSKTSVTV IEENAKAATT ASMEYHSQQD GKASYAVVKN PEVAIGNSWR
IEF
//
