ID A0A0G4PSW1_PENC3 Unreviewed; 959 AA.
AC A0A0G4PSW1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 28-JAN-2026, entry version 46.
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=PCAMFM013_S036g000049 {ECO:0000313|EMBL:CRL29465.1};
OS Penicillium camemberti (strain FM 013).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL29465.1, ECO:0000313|Proteomes:UP000053732};
RN [1] {ECO:0000313|EMBL:CRL29465.1, ECO:0000313|Proteomes:UP000053732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG793169; CRL29465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4PSW1; -.
DR STRING; 1429867.A0A0G4PSW1; -.
DR Proteomes; UP000053732; 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.
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:UP000053732};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..959
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005195709"
FT DOMAIN 96..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 832..869
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 959 AA; 108946 MW; 843763C0B953A547 CRC64;
MARSLPAPRW AMLLSLVILL GCIVVPGLAV KHKDFKTCEQ SGFCKRNRAY ADNASSQGTS
WSSPYELDPA TIHFKDGILT GVISKTTTAN EKVRLPLTVS FLESGAARIV VDEEKRMKGD
IEMRHGSQAN KKRYDETEKW AIVGGLEVSK SATLNAQTET GFTNILYGPG DKFQAIVRHA
PFGVEFQRDG ETHVQLNHQG FLNLEHWRPK VDGKDGESGE DEGTWWEETF GGNTDSKPRG
PESVALDITF PGYNHVFGIP EHADSLSLKE TRGGSGNHEN PYRLYNSDVF EYELESPMTL
YGAIPLMQAH RKNSTVGVFW LNAAETWIDI VKSTASSNPL ALGARSKTDT HTHWISESGQ
IDLFVFLGPS PNDISKTYGE LTGYTQLPQQ FAIGYHQCRW NYVTDEDVKE VNAKFDKYQI
PYDVIWLDLE YTDDRKYFTW DSLTFPDPKG MQQKLDETER KLVVLIDPHI KNADKYFVSE
ELRSKKLAVL NKDGEIYDGW CWPGSSNWVD CFNPAAQAWW ATLHKFDKFK GSLQNLFIWN
DMNEPSVFNG PDMTMPKDNL HYGNWEHRDI HNLNGLTLLD ATYKAMLERK KGEVRRPFIL
TRSYYSGAQR VSAMWTGDNQ ATWEHLGASL PMVLTNGIAG FPFAGADVGG FFHNPDKDLL
TRWYQTGIWY PFFRAHAHID TRRREPYLIS EPQRSYIAQA IRLRYQLMPA WYTAFHEASV
NGTPIVRPQY YMFPEDEQGF AIDDQLYLGS TGLLVKPVVQ ENTYTADVYI SDDEKYYDYF
DFTVYQGAGK KHTVPAPEEK VPVLIQGGHI IPRKDRPRRS TGLMRWDPYT LVITLDKNSE
AEGTLYVDDG ETFDYERGAY IHRRFNYRES VLSSEDIGTK GSKTAEYLKT MTGVTVERVV
IVDPPVEWKT KNTVTVIEDG AKSASTASLE FYEQEGGKAS YVVVKNPNVG IGKAWRIEF
//
