ID MNS1B_EMENI Reviewed; 505 AA. AC Q5BF93; C8VQU4; Q1HFV5; Q9HF85; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 24-JAN-2024, entry version 102. DE RecName: Full=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=AN0787; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Nidulantes. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=SM222; RX PubMed=10974561; DOI=10.1016/s0378-1119(00)00298-5; RA Eades C.J., Hintz W.E.; RT "Characterization of the class I alpha-mannosidase gene family in the RT filamentous fungus Aspergillus nidulans."; RL Gene 255:25-34(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16844780; DOI=10.1073/pnas.0604632103; RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.; RT "Development and application of a suite of polysaccharide-degrading enzymes RT for analyzing plant cell walls."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT effort."; RL Fungal Genet. Biol. 46:S2-13(2009). 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). CC {ECO:0000269|PubMed:10974561}. 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}. CC -!- SEQUENCE CAUTION: CC Sequence=EAA65617.1; Type=Erroneous gene model prediction; Evidence={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; AF129496; AAG48159.1; -; Genomic_DNA. DR EMBL; DQ490469; ABF50845.1; -; mRNA. DR EMBL; AACD01000013; EAA65617.1; ALT_SEQ; Genomic_DNA. DR EMBL; BN001308; CBF88785.1; -; Genomic_DNA. DR RefSeq; XP_658391.1; XM_653299.1. DR AlphaFoldDB; Q5BF93; -. DR SMR; Q5BF93; -. DR STRING; 227321.Q5BF93; -. DR CAZy; GH47; Glycoside Hydrolase Family 47. DR GlyCosmos; Q5BF93; 3 sites, No reported glycans. DR EnsemblFungi; CBF88785; CBF88785; ANIA_00787. DR KEGG; ani:AN0787.2; -. DR VEuPathDB; FungiDB:AN0787; -. DR eggNOG; KOG2204; Eukaryota. DR HOGENOM; CLU_003818_0_2_1; -. DR InParanoid; Q5BF93; -. DR OMA; PESFGWD; -. DR OrthoDB; 1331861at2759; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000000560; Chromosome VIII. DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central. 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 2: Evidence at transcript level; KW Carbohydrate metabolism; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..505 FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B" FT /id="PRO_0000394823" FT ACT_SITE 368 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P31723" FT BINDING 494 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P32906" FT CARBOHYD 88 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 359 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 325..354 FT /evidence="ECO:0000250|UniProtKB:P32906" FT CONFLICT 10 FT /note="L -> F (in Ref. 1; AAG48159)" FT /evidence="ECO:0000305" FT CONFLICT 420 FT /note="R -> L (in Ref. 1; AAG48159)" FT /evidence="ECO:0000305" SQ SEQUENCE 505 AA; 55881 MW; EC77168E8C363B6F CRC64; MRTLLALAAL AGFAAARVPA YAITRPVMRS DSRADAVKEA FSHAWDGYYN YAFPHDELHP ISNGYGDSRN HWGASAVDAL STAIMMRNAT IVNQILDHIA AVDYSKTNAM VSLFETTIRY LAGMISGYDL LKGPAAGLVD DSRVDVLLEQ SQNLAEVLKF AFDTPSGVPY NMINITSGGN DGATTNGLAV TGTLVLEWTR LSDLTGNDEY ARLSQRAEDY LLHPEPAQYE PFPGLIGSAV NIADGKLANG HISWNGGADS YYEYLIKMYV YDPERFGLYR DRWVAAAESS INHLASHPST RPDVTFLATY NEEHQLGLTS QHLTCFDGGS FLLGGTLLDR QDFVDFGLDL VAGCHETYNS TLTGIGPEQF SWDPNGVPDS QKELFERAGF YINSGQYILR PEVIESFYYA WRVTGDGTYR EWVWNAFTNI NKYCRTATGF AGLENVNAAN GGGRIDNQES FMFAEVLKYS FLTFAPEDDW QVQKGSGNTF VYNTEAHPFK VYTPQ //