MNS1B_ASPFC
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 03-AUG-2022, entry version 62.
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 Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
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=CEA10 / CBS 144.89 / FGSC A1163;
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)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-
CC glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
CC Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:139493; EC=3.2.1.113;
CC 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 alpha-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 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 Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 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
