Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P31723 (MAN12_PENCI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

EC=3.2.1.113
Alternative name(s):
Man(9)-alpha-mannosidase
Gene names
Name:MSDC
OrganismPenicillium citrinum
Taxonomic identifier5077 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length511 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 trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Miscellaneous

The enzyme is inactivated by reaction of carbodiimide reagents with Asp-375. Since the antibiotic 1-deoxymannojirimycin (DMM) acts as a competitive inhibitor, and it blocks the reaction with carbodiimides, Asp-375 is established as an active site. High activity in presence of EDTA.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processprotein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Ref.2
Chain36 – 511476Mannosyl-oligosaccharide alpha-1,2-mannosidase
PRO_0000012085

Sites

Active site3751Proton donor

Amino acid modifications

Glycosylation1821N-linked (GlcNAc...)
Glycosylation3661N-linked (GlcNAc...)
Glycosylation4381N-linked (GlcNAc...)
Disulfide bond332 ↔ 361

Experimental info

Sequence conflict4071R → H AA sequence Ref.2

Secondary structure

.................................................................................. 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31723 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: DCBDEBA5768E7596

FASTA51156,570
        10         20         30         40         50         60 
MRLPVSFPLT VLSLLGSTIA HPYGETEAVL RSEPKSNQAK ADAVKEAFQH AWNGYMKYAF 

        70         80         90        100        110        120 
PHDELTPVSN GHADSRNGWG ASAVDALSTA VIMGKADVVN AILEHVADID FSKTSDTVSL 

       130        140        150        160        170        180 
FETTIRYLAG MLSGYDLLQG PAKNLVDNQD LIDGLLDQSR NLADVLKFAF DTPSGVPYNN 

       190        200        210        220        230        240 
INITSHGNDG ATTNGLAVTG TLVLEWTRLS DLTGDEEYAK LSQKAESYLL KPQPSSSEPF 

       250        260        270        280        290        300 
PGLVGSSINI NDGQFADSRV SWNGGDDSFY EYLIKMYVYD PKRFETYKDR WVLAAESTIK 

       310        320        330        340        350        360 
HLKSHPKSRP DLTFLSSYSN RNYDLSSQHL TCFDGGSFLL GGTVLDRQDF IDFGLELVDG 

       370        380        390        400        410        420 
CEATYNSTLT KIGPDSWGWD PKKVPSDQKE FYEKAGFYIS SGSYVLRPEV IESFYYAHRV 

       430        440        450        460        470        480 
TGKEIYRDWV WNAFVAINST CRTDSGFAAV SDVNKANGGS KYDNQESFLF AEVMKYSYLA 

       490        500        510 
HSEDAAWQVQ KGGKNTFVYN TEAHPISVAR N 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the genomic DNA for 1,2-alpha-D-mannosidase gene, msdC from Penicillium citrinum."
Yoshida T., Ichishima E.
Biochim. Biophys. Acta 1263:159-162(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"1,2-alpha-D-mannosidase from Penicillium citrinum: molecular and enzymic properties of two isoenzymes."
Yoshida T., Inoue T., Ichishima E.
Biochem. J. 290:349-354(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-49; 77-94 AND 405-415.
[3]"Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes."
Lobsanov Y.D., Vallee F., Imberty A., Yoshida T., Yip P., Herscovics A., Howell P.L.
J. Biol. Chem. 277:5620-5630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45839 Genomic DNA. Translation: BAA08275.1.
PIRS30362.
S58766.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKTX-ray2.20A/B1-511[»]
1KREX-ray2.20A/B1-511[»]
1KRFX-ray2.20A/B1-511[»]
2RI8X-ray2.16A/B36-510[»]
2RI9X-ray1.95A/B36-510[»]
ProteinModelPortalP31723.
SMRP31723. Positions 36-510.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.
mycoCLAPMSD47C1_PENCI.
MSD47C2_PENCI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP31723.

Entry information

Entry nameMAN12_PENCI
AccessionPrimary (citable) accession number: P31723
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: November 13, 2013
This is version 88 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries