ID A0A2H3IKJ8_9EURO Unreviewed; 1273 AA.
AC A0A2H3IKJ8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000256|ARBA:ARBA00038888, ECO:0000256|RuleBase:RU368089};
DE EC=3.2.1.106 {ECO:0000256|ARBA:ARBA00038888, ECO:0000256|RuleBase:RU368089};
DE AltName: Full=Glucosidase I {ECO:0000256|RuleBase:RU369107};
GN ORFNames=PENO1_023990 {ECO:0000313|EMBL:PCH05179.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH05179.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH05179.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH05179.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
CC {ECO:0000256|RuleBase:RU368089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC ChEBI:CHEBI:132537; EC=3.2.1.106;
CC Evidence={ECO:0000256|RuleBase:RU368089};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|RuleBase:RU369107}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648,
CC ECO:0000256|RuleBase:RU368089}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family.
CC {ECO:0000256|ARBA:ARBA00010833, ECO:0000256|RuleBase:RU368089}.
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:PCH05179.1}.
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DR EMBL; NPFK01000044; PCH05179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IKJ8; -.
DR STRING; 290292.A0A2H3IKJ8; -.
DR OrthoDB; 1571at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.70.98.110; Glycosyl hydrolase family 63, N-terminal domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR031335; Glyco_hydro_63_C.
DR InterPro; IPR031631; Glyco_hydro_63N.
DR InterPro; IPR038518; Glyco_hydro_63N_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR PANTHER; PTHR10412:SF11; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368089};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU369107};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU368089};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368089};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 9..380
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 494..722
FT /note="Glycosyl hydrolase family 63 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16923"
FT DOMAIN 761..1260
FT /note="Glycosyl hydrolase family 63 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03200"
FT REGION 651..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 142042 MW; 51F1FD9C0598FA67 CRC64;
MASDKERNIV IIGGGIIGSC SAYYLTRHPS YNPSLHKITL LEASEIAGGA SGKAGGLLAL
WAYPSSIVPL SYKLHAELAK EHNGKDNWGY REVNCGQLIV KGRAVDKKDD AGSVSLQKRD
AAAIGKLRAA GIPTDLDWLL SDGIRGYESM SGPGETAQVH PYQFTTSIAK LAEEKGVKIV
LGTVTKINSE ADSVQSVTYT DKASGESHTL PATDVIVSAG PWTKRVLPSA PISATRAHSV
VIKPTRPISA YTLFTNIELP SKHNPKRSTV ETPEIYARPD ATVYACGDGD HIVPLPDTTA
DVEVDPKRCQ DIIDSVGSIS DELRQGEIVK QQACYLPNVD ARGGGGPLIG HSGTKGLYVA
TGHTCWGIQN APGTGKLIID IEAQINSRRN AEHKRKRYVE SPQRPITIAP SICHLYTYTS
QPHNFHKAAA QSIEEANTQL PLILTDALLV GYTRKMHLQF SFYLLWSSFV VGCAYGANDV
SVLINEVAKA NNQSLLWGPY KPNLYFGVRP RIPKSLTAGL MWAKVDNYAT AQANFRHTCE
QNEGMRGYGW DEYDVRKGGR QSIHDVGNSI DLTIDFVKVP GGLHGGSWAA RVKGTPREDA
PEDLYTSLVF YASLEGLGSL HVDNAVEQQM GLKEDVKLKG MTPELGDFKL SITTGPDSNK
HPEFDHPSSA EKSLDRPLVA SVETPQENLW QAKALMFTAM KPEVEGLIAK YGTDAPPPPA
QLFTVPNHPG TGNIHFVQHV FEGAFEFDIL FESGSAPEPV TSETLTEKID EMSSSFSSRY
ENVFAPQAPF EKAEYSEFSK SMFSNLVGGI GYFYGSGLVD RSEAPEYEEE NEGFWEEAAE
ARSRVQPTEE DPRELFTSIP SRPFFPRGFL WDEGFHLIPI VDWDLDLTLD IVQSWFNLMD
EDGWIAREQI LGAEARSKVP PEFTVQYPHY ANPPTLFMVL EAFVDKLQAN QSIIENFELN
RADIADSLRS AHLESKELAE SYLHAIYPLL RRQYFWFKKT QWGDVKSYDR EAYSSKEAYR
WRGRTVRHIL TSGLDDYPRA QPPHPGELHT DLISWMGLMS RSLRKIAAAI GETDDAEEFA
IYEYAITRNI DDLHWDEDAQ TWCDATIDEY EESVHVCHKG YISIFPFLTG MVGPDSPHLK
ATLDLIRNSN ELWSDYGIRS LSKNDEFYGT DENYWRSPIW MNMNYMIVKN LYEIATSSSP
HKAQATEIYN DLRKNLVENV FREWKDTGFA WEQYNPETGK GQRTQHFTGW TSLVVKIMNM
PYLTVSGRGH DEL
//
