MNS1_CANAX
ID MNS1_CANAX Reviewed; 565 AA.
AC Q8J0Q0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase;
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Man(9)-alpha-mannosidase;
GN Name=MNS1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26555;
RA Mora-Montes H.M., Flores-Carreon A., Ponce-Noyola P., Lopez-Romero E.,
RA Zinker-Ruzal S.;
RT "Identification of the alpha1,2-mannosidase gene (Mns1) in Candida
RT albicans.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC Trim a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to
CC produce Man(8)GlcNAc(2) (By similarity). {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:P45700};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; AY167027; AAN86059.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8J0Q0; -.
DR SMR; Q8J0Q0; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR VEuPathDB; FungiDB:C1_03730C_A; -.
DR VEuPathDB; FungiDB:CAWG_01018; -.
DR BRENDA; 3.2.1.113; 1096.
DR BRENDA; 3.2.1.209; 1096.
DR UniPathway; UPA00378; -.
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:InterPro.
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 Calcium; Disulfide bond; Glycosidase; Hydrolase; Metal-binding.
FT CHAIN 1..565
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase"
FT /id="PRO_0000210318"
FT REGION 526..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
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 DISULFID 320..363
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 565 AA; 64659 MW; C3581A0D889CCAF2 CRC64;
MLLKGFMLSL VLYAVYHLAS NGGQFMFDFS GQSKWERAQS EVRQAILDSW HTYEKYGWGY
DVYHPIKQEG ENMGPKPLGW MIVDSLDTLM IMDCPEEVSR ARDWIKNDLD YTFDYNVNTF
ETTIRMLGGL LSAYHFSNDD VYLDKAVQLA NALHGAYDSP SGIPYSSVNL KSGKGIKNHV
DNGASSTAEA ATVQLEMKYL SKLTGEILWW NLAEKVMQVL ESNKPQDGLV PIYVNPDTGK
YQGHLIRLGS RGDSYYEYLL KQYLQTNKQE LVYWDMYRES VEGVKKHLVS DSYPSGLTFI
GELDNGIGGK LSTKMDHLVC FYGGLLALGA TGGLTLNEAQ SLKSWNEERE ADFKLGEELT
YTCYKMYHDV SPTGLSPEIV VFNEDTSKSK DFIIKPLDRH NLQRPETVES LFYLYRLTGD
VKYREMGYEI FQNFIKYTKV VNSEGEVSFS SLSDVTSFDS NGLPKFKDNT ESFWWAETLK
YLYLLFDDTN KIPLTDYVFN TEAHPFPRFD TNDYFKTGWR RKIDENEKAQ MRESKVIDKS
NLPEAQPVDK SADQEAKEII EEIAG
