Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q2ULB2 (MNS1B_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	mns1B
Synonyms:	manA, msdS
ORF Names:	AO090003000476

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasmic vesicle
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasmic membrane-bounded vesicle lumen Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

21

Potential

Chain

489

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

PRO_0000394820

Sites

Active site

1

Proton donor By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2ULB2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5F24FEDB0B43F2BF
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510

56,631

        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

References

	« Hide 'large scale' referencesShow '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. 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.
RefSeq	XP_001819655.1. XM_001819603.1.
3D structure databases
ProteinModelPortal	Q2ULB2.
SMR	Q2ULB2. Positions 36-509.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00001087.
Protein family/group databases
mycoCLAP	MSD47A2_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00001104; CADAORAP00001087; CADAORAG00001104.
GeneID	5991638.
KEGG	aor:AOR_1_2802154.
Phylogenomic databases
eggNOG	NOG300315.
HOGENOM	HOG000181987.
KO	K01230.
OrthoDB	EOG42JS14.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
Gene3D	1.50.10.50. 1 hit.
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
PANTHER	PTHR11742. PTHR11742. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MNS1B_ASPOR

Accession

Primary (citable) accession number: Q2ULB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

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

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents