ID   MNS1B_ASPFC             Reviewed;         493 AA.
AC   B0XMT4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B;
DE            EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE   AltName: Full=Class I alpha-mannosidase 1B;
DE   AltName: Full=Man(9)-alpha-mannosidase 1B;
DE   Flags: Precursor;
GN   Name=mns1B; Synonyms=msdS; ORFNames=AFUB_014090;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC       Progressively trims alpha-1,2-linked mannose residues from
CC       Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC         mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->3)-[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] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008,
CC         Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493;
CC         EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC         8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC         (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
CC         (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC         COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC         EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC       Note=Ca(2+). Can also use Mg(2+), but with lower efficiency.
CC       {ECO:0000250|UniProtKB:Q2ULB2};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P32906}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR   EMBL; DS499594; EDP56691.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XMT4; -.
DR   SMR; B0XMT4; -.
DR   Allergome; 8990; Asp f Mannosidase.
DR   GlyCosmos; B0XMT4; 3 sites, No reported glycans.
DR   EnsemblFungi; EDP56691; EDP56691; AFUB_014090.
DR   VEuPathDB; FungiDB:AFUB_014090; -.
DR   HOGENOM; CLU_003818_0_2_1; -.
DR   PhylomeDB; B0XMT4; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProt.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR036026; Seven-hairpin_glycosidases.
DR   PANTHER; PTHR11742:SF101; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE 1B; 1.
DR   PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..493
FT                   /note="Probable mannosyl-oligosaccharide alpha-1,2-
FT                   mannosidase 1B"
FT                   /id="PRO_0000394817"
FT   ACT_SITE        367
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P31723"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        324..353
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
SQ   SEQUENCE   493 AA;  53840 MW;  AB055CB6591E76CC CRC64;
     MHLPSLSVAL ALVSSSLALP QAVLPENDVS SRAAAVKEAF SHAWDGYMKY AFPHDELLPV
     SNSYGDSRNG WGASAVDALS TAIVMRNATI VSQILDHIAK IDYSKTSDMV SLFETTIRYL
     GGMLSGYDLL KGPAADLVED RTKVDMLLQQ SKNLGDVLKF AFDTPSGVPY NNINITSHGN
     DGATTNGLAV TGTLVLEWTR LSDLTGDQEY AKLSQRAESY LLAPQPSSGE PFPGLVGSAI
     SIQTGQFTNG FVSWNGGSDS FYEYLMKMYV YDPKRFATYK DRWVAAAESS IDHLASNPAS
     RPDLTFLATY NKGSLGLSSQ HLACFDGGSY LLGGTVLDRA DLIDFGLKLV DGCAETYHQT
     LTGIGPESFG WDEKSVPADQ KELYERAGFY VQSGAYILRP EVIESFYYAY RVTGKKQYRD
     WVWNAFENIN KYCRTESGFA GLTNVNAVNG GGRYDNQESF LFAEVMKYAY LTHAPGMSSM
     PAAAEDKANK SRG
//