MNS1B_NEOFI
ID MNS1B_NEOFI Reviewed; 493 AA.
AC A1D1W1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=NFIA_010860;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027688; EAW22404.1; -; Genomic_DNA.
DR RefSeq; XP_001264301.1; XM_001264300.1.
DR AlphaFoldDB; A1D1W1; -.
DR SMR; A1D1W1; -.
DR STRING; 36630.CADNFIAP00001081; -.
DR PRIDE; A1D1W1; -.
DR EnsemblFungi; EAW22404; EAW22404; NFIA_010860.
DR GeneID; 4591109; -.
DR KEGG; nfi:NFIA_010860; -.
DR VEuPathDB; FungiDB:NFIA_010860; -.
DR eggNOG; KOG2204; Eukaryota.
DR HOGENOM; CLU_003818_0_2_1; -.
DR OMA; LIKMYLY; -.
DR OrthoDB; 434316at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000006702; 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; Reference proteome; 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_0000394824"
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; 53855 MW; 8E6C4E050EA8E4CB CRC64;
MHLPSLSVAL ALVSSSLALP QTVLPESDVS SHAAAVKEAF SHAWDGYMKY AFPHDELLPI
SNSYGDSRNG WGASAVDALS TAIVMRNATI VNQILDHIAK IDYSKTSDTV SLFETTIRYL
GGMLSGYDLL KGPAADLVKD STKVDMLLQQ SKNLGDVLKF AFDTPSGVPY NNINITSHGN
DGATTNGLAV TGTLVLEWTR LSDLTGDQEY AKLSQRAESY LLAPQPSSGE PFPGLVGSEI
SIQTGQFTNG FVSWNGGSDS FYEYLMKMYV YDPKRFATYK DRWVAAAESS IDHLASSPAS
RPDLTFLATY NKGSLGLSSQ HLACFDGGSY LLGGTVLDRA DLIDFGLKLV DGCAETYHQT
LTGIGPESFG WDEKSVPADQ KEFYERAGFY VQSGAYILRP EVIESFYYAY RVTGKKQYRD
WVWNAFVNIN KYCRTGSGFA GLTDVNAVNG GNRYDNQESF LFAEVMKYAY LTHAPGMSPI
SIADEDKANE SRG
