ID MNS1B_ASPCL Reviewed; 511 AA. AC A1CP08; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 04-NOV-2026, entry version 89. 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=ACLA_020870; OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / OS NRRL 1 / QM 1276 / 107). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=344612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 RC / 107; 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=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)- CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D- CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan CC mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)- CC [alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D- CC Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl- CC [protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose; 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=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]- CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- CC GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) CC + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[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 5A1,2) + 3 beta-D-mannose; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS027059; EAW07379.1; -; Genomic_DNA. DR RefSeq; XP_001268805.1; XM_001268804.1. DR SMR; A1CP08; -. DR STRING; 344612.A1CP08; -. DR GlyCosmos; A1CP08; 3 sites, No reported glycans. DR EnsemblFungi; EAW07379; EAW07379; ACLA_020870. DR GeneID; 4701674; -. DR KEGG; act:ACLA_020870; -. DR VEuPathDB; FungiDB:ACLA_020870; -. DR eggNOG; KOG2204; Eukaryota. DR HOGENOM; CLU_003818_0_2_1; -. DR OMA; AACHETY; -. DR OrthoDB; 8118055at2759; -. DR UniPathway; UPA00378; -. DR FunFam; 1.50.10.10:FF:000047; Mannosyl-oligosaccharide alpha-1,2-mannosidase; 1. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR001382; Glyco_hydro_47. DR InterPro; IPR050749; Glycosyl_Hydrolase_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. DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter. 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; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0036503; P:ERAD pathway; IEA:UniProtKB-ARBA. DR Proteomes; UP000006701; Unassembled WGS sequence. DR AlphaFoldDB; A1CP08; -. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..511 FT /note="Probable mannosyl-oligosaccharide alpha-1,2- FT mannosidase 1B" FT /id="PRO_0000394816" FT ACT_SITE 370 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P31723" FT BINDING 501 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P32906" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 327..356 FT /evidence="ECO:0000250|UniProtKB:P32906" SQ SEQUENCE 511 AA; 56325 MW; F13A052EC4FDD714 CRC64; MHLPSLSLAW ALAGSSLALP QAEQPVLQDD RASSRAAAVK EAFSHAWDGY KKYAFPHDEL HPISNGYGNS RNGWGASAVD ALSTAIVMRN ATIVHEILDH IATIDYSKTS DTVSLFETTI RYLGGMLSGY DLLKGPAADL VKDTSKVDIL LKQSKNLGDI LKFAFDTPSG VPYNNINITS HGHDGAKTNG LAVTGTLVLE WTRLSDLTGD PEYAQLSQKA ESYLLHPQPS SAEPFPGLIG SNIDIKTGQF TDGHVSWNGG DDSYYEYLIK MYVYDPTRFA LYRDRWVAAA ESSIEHLASH PASRPDLTFL ATYDGGRYGL SSQHLACFDG GNFLLGGTVL DRRDLIDFGL ALVDACHETY SQTLTGIGPE SFGWDANSVP ADQKELYERA GFYVQNGAYI LRPEVIESFY YAWRVTGRSE YRDWVWTAFV AINKTCRTGS GYAGLTNVNA ENGGGRYDNQ ESFLFAEVLK YAYLTHSEEL MAAEDAWQVQ RGDGNQFVFN TEAHPIRVHH S //