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Protein

Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B

Gene

mns1B

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.1 Publication

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactori

Ca2+1 Publication, Mg2+1 PublicationNote: Ca(2+). Can also use Mg2+, but with lower efficiency.1 Publication

pH dependencei

Optimum pH is 5.5. Activity is above 50 percent between pH 4.5 and 6.5.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Activity remains at about 60 percent and 14 percent at 60 degrees Celsius and 65 degrees Celsius respectively.1 Publication

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 3751Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

mycoCLAPiMSD47A2_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B (EC:3.2.1.113)
Alternative name(s):
Class I alpha-mannosidase 1B
Man(9)-alpha-mannosidase 1B
Gene namesi
Name:mns1B
Synonyms:manA, msdS
ORF Names:AO090003000476
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 510489Mannosyl-oligosaccharide alpha-1,2-mannosidase 1BPRO_0000394820Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi332 ↔ 361By similarity
Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi5062.CADAORAP00001087.

Structurei

3D structure databases

ProteinModelPortaliQ2ULB2.
SMRiQ2ULB2. Positions 36-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181987.
KOiK01230.
OMAiGPESFGW.
OrthoDBiEOG7BP8BH.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2ULB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHFSSLSLPL TALSLVTPSL AYPQFKFEQR VARSNSSESR ANAVKEAFVH
60 70 80 90 100
AWDGYMQYAY PHDELHPISN GVGDSRNGWG ASAVDALSTA VIMGNETIVN
110 120 130 140 150
QILDHIATID YSKTDDQVSL FETTIRYLGG MLSGYDLLKG PASNLVKDQA
160 170 180 190 200
KVKTLLDQSQ NLADVLKFAF DTPSGIPYNN INITSHGNDG ATTNGLAVTG
210 220 230 240 250
TLVLEWTRLS DLTGDTEYAQ LSQKAEDYLL NPSPKSAEPF EGLVGSHINI
260 270 280 290 300
SNGAFADGQV SWNGGDDSFY EYLIKMYVYD PKRFSTYGDR WVKAAESSIK
310 320 330 340 350
HLASHPEKRP DLTFLASYND GQYGLSSQHL TCFDGGSFLL GGTVLDRDDF
360 370 380 390 400
IQFGLDLVKG CHETYNQTLT GIGPESFGWD PKNVPSDQKE LYERAGFYIS
410 420 430 440 450
SGAYILRPEV IESFYYAWRI TGQEIYREWV WNAFVNINKY CRTDSGFAGL
460 470 480 490 500
TNVNAANGGG RYDNQESFLF AEVLKYVYLT FAPDNEWQVQ RGKGNKFVYN
510
TEAHPVRVAA
Length:510
Mass (Da):56,631
Last modified:January 24, 2006 - v1
Checksum:i5F24FEDB0B43F2BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069647 Genomic DNA. Translation: BAC07247.1.
AP007155 Genomic DNA. Translation: BAE57653.1.
RefSeqiXP_001819655.1. XM_001819603.1.

Genome annotation databases

EnsemblFungiiCADAORAT00001104; CADAORAP00001087; CADAORAG00001104.
GeneIDi5991638.
KEGGiaor:AOR_1_2802154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069647 Genomic DNA. Translation: BAC07247.1.
AP007155 Genomic DNA. Translation: BAE57653.1.
RefSeqiXP_001819655.1. XM_001819603.1.

3D structure databases

ProteinModelPortaliQ2ULB2.
SMRiQ2ULB2. Positions 36-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00001087.

Protein family/group databases

mycoCLAPiMSD47A2_ASPOR.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00001104; CADAORAP00001087; CADAORAG00001104.
GeneIDi5991638.
KEGGiaor:AOR_1_2802154.

Phylogenomic databases

eggNOGiNOG300315.
HOGENOMiHOG000181987.
KOiK01230.
OMAiGPESFGW.
OrthoDBiEOG7BP8BH.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of 1,2-alpha-mannosidase gene (fmanIB) from filamentous fungus Aspergillus oryzae: in vivo visualization of the FmanIBp-GFP fusion protein."
    Akao T., Yamaguchi M., Yahara A., Yoshiuchi K., Fujita H., Yamada O., Akita O., Ohmachi T., Asada Y., Yoshida T.
    Biosci. Biotechnol. Biochem. 70:471-479(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    Strain: ATCC 42149 / RIB 40.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiMNS1B_ASPOR
AccessioniPrimary (citable) accession number: Q2ULB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: April 1, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.