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UniProtKB - Q5BF93 (MNS1B_EMENI)
Protein
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
Gene
mns1B
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Functioni
Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.
1 PublicationCatalytic activityi
- 4 H2O + N4-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 β-D-mannose + N4-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)By similarityEC:3.2.1.113By similarity
- 3 H2O + N4-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 β-D-mannose + N4-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)By similarityEC:3.2.1.113By similarity
Cofactori
Ca2+By similarity, Mg2+By similarityNote: Ca2+. Can also use Mg2+, but with lower efficiency.By similarity
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarityView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 368 | Proton donorBy similarity | 1 | |
Metal bindingi | 494 | CalciumBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: GO_Central
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-KW
- N-glycan processing Source: GO_Central
- protein glycosylation Source: UniProtKB-UniPathway
- ubiquitin-dependent ERAD pathway Source: GO_Central
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism |
Ligand | Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GH47, Glycoside Hydrolase Family 47 |
Names & Taxonomyi
Protein namesi | Recommended name: Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B (EC:3.2.1.113By similarity)Alternative name(s): Class I alpha-mannosidase 1B Man(9)-alpha-mannosidase 1B |
Gene namesi | Name:mns1B Synonyms:msdS ORF Names:AN0787 |
Organismi | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic identifieri | 227321 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Nidulantes › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:AN0787 |
Subcellular locationi
Other locations
- Cytoplasmic vesicle lumen By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: GO_Central
Golgi apparatus
- Golgi membrane Source: GO_Central
Other locations
- cytoplasmic vesicle lumen Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasmic vesiclePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 16 | Sequence analysisAdd BLAST | 16 | |
ChainiPRO_0000394823 | 17 – 505 | Mannosyl-oligosaccharide alpha-1,2-mannosidase 1BAdd BLAST | 489 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 88 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 174 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 325 ↔ 354 | By similarity | ||
Glycosylationi | 359 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PRIDEi | Q5BF93 |
Interactioni
Subunit structurei
Monomer.
By similarityProtein-protein interaction databases
STRINGi | 227321.Q5BF93 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyl hydrolase 47 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG2204, Eukaryota |
HOGENOMi | CLU_003818_0_2_1 |
InParanoidi | Q5BF93 |
OMAi | YSYLIHA |
OrthoDBi | 434316at2759 |
Family and domain databases
Gene3Di | 1.50.10.10, 1 hit |
InterProi | View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases |
Pfami | View protein in Pfam PF01532, Glyco_hydro_47, 1 hit |
PRINTSi | PR00747, GLYHDRLASE47 |
SUPFAMi | SSF48225, SSF48225, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q5BF93-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRTLLALAAL AGFAAARVPA YAITRPVMRS DSRADAVKEA FSHAWDGYYN
60 70 80 90 100
YAFPHDELHP ISNGYGDSRN HWGASAVDAL STAIMMRNAT IVNQILDHIA
110 120 130 140 150
AVDYSKTNAM VSLFETTIRY LAGMISGYDL LKGPAAGLVD DSRVDVLLEQ
160 170 180 190 200
SQNLAEVLKF AFDTPSGVPY NMINITSGGN DGATTNGLAV TGTLVLEWTR
210 220 230 240 250
LSDLTGNDEY ARLSQRAEDY LLHPEPAQYE PFPGLIGSAV NIADGKLANG
260 270 280 290 300
HISWNGGADS YYEYLIKMYV YDPERFGLYR DRWVAAAESS INHLASHPST
310 320 330 340 350
RPDVTFLATY NEEHQLGLTS QHLTCFDGGS FLLGGTLLDR QDFVDFGLDL
360 370 380 390 400
VAGCHETYNS TLTGIGPEQF SWDPNGVPDS QKELFERAGF YINSGQYILR
410 420 430 440 450
PEVIESFYYA WRVTGDGTYR EWVWNAFTNI NKYCRTATGF AGLENVNAAN
460 470 480 490 500
GGGRIDNQES FMFAEVLKYS FLTFAPEDDW QVQKGSGNTF VYNTEAHPFK
VYTPQ
Sequence cautioni
The sequence EAA65617 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 10 | L → F in AAG48159 (PubMed:10974561).Curated | 1 | |
Sequence conflicti | 420 | R → L in AAG48159 (PubMed:10974561).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF129496 Genomic DNA Translation: AAG48159.1 DQ490469 mRNA Translation: ABF50845.1 AACD01000013 Genomic DNA Translation: EAA65617.1 Sequence problems. BN001308 Genomic DNA Translation: CBF88785.1 |
RefSeqi | XP_658391.1, XM_653299.1 |
Genome annotation databases
EnsemblFungii | CBF88785; CBF88785; ANIA_00787 EAA65617; EAA65617; AN0787.2 |
GeneIDi | 2876566 |
KEGGi | ani:AN0787.2 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF129496 Genomic DNA Translation: AAG48159.1 DQ490469 mRNA Translation: ABF50845.1 AACD01000013 Genomic DNA Translation: EAA65617.1 Sequence problems. BN001308 Genomic DNA Translation: CBF88785.1 |
RefSeqi | XP_658391.1, XM_653299.1 |
3D structure databases
SMRi | Q5BF93 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 227321.Q5BF93 |
Protein family/group databases
CAZyi | GH47, Glycoside Hydrolase Family 47 |
Proteomic databases
PRIDEi | Q5BF93 |
Genome annotation databases
EnsemblFungii | CBF88785; CBF88785; ANIA_00787 EAA65617; EAA65617; AN0787.2 |
GeneIDi | 2876566 |
KEGGi | ani:AN0787.2 |
Organism-specific databases
VEuPathDBi | FungiDB:AN0787 |
Phylogenomic databases
eggNOGi | KOG2204, Eukaryota |
HOGENOMi | CLU_003818_0_2_1 |
InParanoidi | Q5BF93 |
OMAi | YSYLIHA |
OrthoDBi | 434316at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
Family and domain databases
Gene3Di | 1.50.10.10, 1 hit |
InterProi | View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases |
Pfami | View protein in Pfam PF01532, Glyco_hydro_47, 1 hit |
PRINTSi | PR00747, GLYHDRLASE47 |
SUPFAMi | SSF48225, SSF48225, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MNS1B_EMENI | |
Accessioni | Q5BF93Primary (citable) accession number: Q5BF93 Secondary accession number(s): C8VQU4, Q1HFV5, Q9HF85 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 15, 2010 |
Last sequence update: | June 15, 2010 | |
Last modified: | February 23, 2022 | |
This is version 92 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families