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Q2ULB2 (MNS1B_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:mns1B
Synonyms:manA, msdS
ORF Names:AO090003000476
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Ca2+. Can also use Mg2+, but with lower efficiency. Ref.1

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasmic vesicle lumen Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Activity is above 50 percent between pH 4.5 and 6.5. Ref.1

Temperature dependence:

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 510489Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
PRO_0000394820

Sites

Active site3751Proton donor By similarity

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Disulfide bond332 ↔ 361 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2ULB2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5F24FEDB0B43F2BF

FASTA51056,631
        10         20         30         40         50         60 
MHFSSLSLPL TALSLVTPSL AYPQFKFEQR VARSNSSESR ANAVKEAFVH AWDGYMQYAY 

        70         80         90        100        110        120 
PHDELHPISN GVGDSRNGWG ASAVDALSTA VIMGNETIVN QILDHIATID YSKTDDQVSL 

       130        140        150        160        170        180 
FETTIRYLGG MLSGYDLLKG PASNLVKDQA KVKTLLDQSQ NLADVLKFAF DTPSGIPYNN 

       190        200        210        220        230        240 
INITSHGNDG ATTNGLAVTG TLVLEWTRLS DLTGDTEYAQ LSQKAEDYLL NPSPKSAEPF 

       250        260        270        280        290        300 
EGLVGSHINI SNGAFADGQV SWNGGDDSFY EYLIKMYVYD PKRFSTYGDR WVKAAESSIK 

       310        320        330        340        350        360 
HLASHPEKRP DLTFLASYND GQYGLSSQHL TCFDGGSFLL GGTVLDRDDF IQFGLDLVKG 

       370        380        390        400        410        420 
CHETYNQTLT GIGPESFGWD PKNVPSDQKE LYERAGFYIS SGAYILRPEV IESFYYAWRI 

       430        440        450        460        470        480 
TGQEIYREWV WNAFVNINKY CRTDSGFAGL TNVNAANGGG RYDNQESFLF AEVLKYVYLT 

       490        500        510 
FAPDNEWQVQ RGKGNKFVYN TEAHPVRVAA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB069647 Genomic DNA. Translation: BAC07247.1.
AP007155 Genomic DNA. Translation: BAE57653.1.
RefSeqXP_001819655.1. XM_001819603.1.

3D structure databases

ProteinModelPortalQ2ULB2.
SMRQ2ULB2. Positions 36-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00001087.

Protein family/group databases

mycoCLAPMSD47A2_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00001104; CADAORAP00001087; CADAORAG00001104.
GeneID5991638.
KEGGaor:AOR_1_2802154.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
KOK01230.
OMAGPESFGW.
OrthoDBEOG7BP8BH.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNS1B_ASPOR
AccessionPrimary (citable) accession number: Q2ULB2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: November 13, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries