MNS1B_ASPOR
ID MNS1B_ASPOR Reviewed; 510 AA.
AC Q2ULB2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=manA, msdS; ORFNames=AO090003000476;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, GLYCOSYLATION,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16495665; DOI=10.1271/bbb.70.471;
RA Akao T., Yamaguchi M., Yahara A., Yoshiuchi K., Fujita H., Yamada O.,
RA Akita O., Ohmachi T., Asada Y., Yoshida T.;
RT "Cloning and expression of 1,2-alpha-mannosidase gene (fmanIB) from
RT filamentous fungus Aspergillus oryzae: in vivo visualization of the
RT FmanIBp-GFP fusion protein.";
RL Biosci. Biotechnol. Biochem. 70:471-479(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:16495665}.
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:0000269|PubMed:16495665};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16495665};
CC Note=Ca(2+). Can also use Mg(2+), but with lower efficiency.
CC {ECO:0000269|PubMed:16495665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Activity is above 50 percent between pH 4.5 and
CC 6.5. {ECO:0000269|PubMed:16495665};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Activity remains at about
CC 60 percent and 14 percent at 60 degrees Celsius and 65 degrees
CC Celsius respectively. {ECO:0000269|PubMed:16495665};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen
CC {ECO:0000269|PubMed:16495665}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; AB069647; BAC07247.1; -; Genomic_DNA.
DR EMBL; AP007155; BAE57653.1; -; Genomic_DNA.
DR RefSeq; XP_001819655.1; XM_001819603.1.
DR AlphaFoldDB; Q2ULB2; -.
DR SMR; Q2ULB2; -.
DR STRING; 510516.Q2ULB2; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR CLAE; MSD47A2_ASPOR; -.
DR EnsemblFungi; BAE57653; BAE57653; AO090003000476.
DR GeneID; 5991638; -.
DR KEGG; aor:AO090003000476; -.
DR VEuPathDB; FungiDB:AO090003000476; -.
DR HOGENOM; CLU_003818_0_2_1; -.
DR OMA; LIKMYLY; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000006564; Chromosome 2.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..510
FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B"
FT /id="PRO_0000394820"
FT ACT_SITE 375
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 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 332..361
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 510 AA; 56631 MW; 5F24FEDB0B43F2BF CRC64;
MHFSSLSLPL TALSLVTPSL AYPQFKFEQR VARSNSSESR ANAVKEAFVH AWDGYMQYAY
PHDELHPISN GVGDSRNGWG ASAVDALSTA VIMGNETIVN QILDHIATID YSKTDDQVSL
FETTIRYLGG MLSGYDLLKG PASNLVKDQA KVKTLLDQSQ NLADVLKFAF DTPSGIPYNN
INITSHGNDG ATTNGLAVTG TLVLEWTRLS DLTGDTEYAQ LSQKAEDYLL NPSPKSAEPF
EGLVGSHINI SNGAFADGQV SWNGGDDSFY EYLIKMYVYD PKRFSTYGDR WVKAAESSIK
HLASHPEKRP DLTFLASYND GQYGLSSQHL TCFDGGSFLL GGTVLDRDDF IQFGLDLVKG
CHETYNQTLT GIGPESFGWD PKNVPSDQKE LYERAGFYIS SGAYILRPEV IESFYYAWRI
TGQEIYREWV WNAFVNINKY CRTDSGFAGL TNVNAANGGG RYDNQESFLF AEVLKYVYLT
FAPDNEWQVQ RGKGNKFVYN TEAHPVRVAA
