ID A0A1E3BIV7_ASPCR Unreviewed; 958 AA.
AC A0A1E3BIV7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
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=SI65_03932 {ECO:0000313|EMBL:ODM20879.1};
OS Aspergillus cristatus (Chinese Fuzhuan brick tea-fermentation fungus)
OS (Eurotium cristatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=573508 {ECO:0000313|EMBL:ODM20879.1, ECO:0000313|Proteomes:UP000094569};
RN [1] {ECO:0000313|EMBL:ODM20879.1, ECO:0000313|Proteomes:UP000094569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GZAAS20.1005 {ECO:0000313|EMBL:ODM20879.1,
RC ECO:0000313|Proteomes:UP000094569};
RX PubMed=27267057; DOI=10.1186/s12864-016-2637-y;
RA Ge Y., Wang Y., Liu Y., Tan Y., Ren X., Zhang X., Hyde K.D., Liu Y.,
RA Liu Z.;
RT "Comparative genomic and transcriptomic analyses of the Fuzhuan brick tea-
RT fermentation fungus Aspergillus cristatus.";
RL BMC Genomics 17:428-428(2016).
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:ODM20879.1}.
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DR EMBL; JXNT01000003; ODM20879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3BIV7; -.
DR STRING; 573508.A0A1E3BIV7; -.
DR VEuPathDB; FungiDB:SI65_03932; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000094569; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000094569};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..958
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009123725"
FT DOMAIN 96..328
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 385..713
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 721..810
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 830..868
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 958 AA; 109192 MW; 39DF60AF4648FCAE CRC64;
MARSWPVSVR WTLLLLVVIL GWLVVPGVTV KRESFKYCSQ SGFCKRNRAY ADEASAKGSS
WSSPYELEPS SIQFKDSQLN GVIIKTTSAN EKVRLPLTVS FLESGAARVV IDEEKRLKGE
IDLRHNSQIR KERYNEAEKW AVVGGLDLSK SATLNANTEE GLTKVLYGPG NSFQAVIRHA
PFDVEFQRDG ETHVQFNKQG YLNMEHWRPK LEPEEDSPED QSTWWEETFD GNTDSKPRGP
ESVALDISFP GYSHVFGIPE HADSLSLRET RGGSGNHEDP YRLYNSDIFE YELNSPMTLY
GAIPLMQAHR KGSTVGVFWL NAAETWIDIV KSSSSVNPLS LGVGPKTTTH SHWISEAGRL
DVFVFLGPTP RDISKTYGEL TGYTQLPQQF AIAYHQCRWN YVTDEDVKEV DAQFDKYQIP
YDVIWLDVDY TDDRKYFTWD PMTFPNPISM EEQLDNSERK LVVLIDPHIK NEEGYFVSEE
MKKQGFAVKN KDGNIYDGHC WPGASNWIDC FNPEAAKWWS TLYRYDKFKG SSPNVFIWND
MNEPSVFDGP EVTMPKDNIH WGNWEHRDIH NVNGVTLLNS TFKALTARKK GENRRPFILT
RSYYAGAQRV AAMWTGDNQA TWDHLAITLS MVLNNGISGF PFAGADVGGF FHNPGPELLT
RWYQTGIWYP FFRAHAHIET RRREPYLISR PHRDYISQAL RLRYQLLPAW YTAFHEASVN
GTPIVRPQFY MHPTDEQGFT LDDQLYFGST GLLTKPVVSE GANSADIYIS DDEKYYDYFD
YTVYQGAKKR HTVPAPIEKV PLLMQGGHVI PRKDRPRRSS GLMKWDPYTL VITLDKNGEA
DGTLYVDDGE SYEYQRGAYI HRNFHFKDSV LSSHDIGTKG PKTAEYLKTM ANVKVEKIIV
IDPPKEWQDK VSVTIIEDGA TTGTTASMQY FSQSTGKAPY AVVKKPDVGI GGTWRIEF
//
