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Protein

Mannosyl-oligosaccharide alpha-1,2-mannosidase

Gene

MSDC

Organism
Penicillium citrinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

pH dependencei

Optimum pH is 5.0.

Pathway:iprotein 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 donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.113. 4608.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.
mycoCLAPiMSD47C1_PENCI.
MSD47C2_PENCI.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide alpha-1,2-mannosidase (EC:3.2.1.113)
Alternative name(s):
Man(9)-alpha-mannosidase
Gene namesi
Name:MSDC
OrganismiPenicillium citrinum
Taxonomic identifieri5077 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35351 PublicationAdd
BLAST
Chaini36 – 511476Mannosyl-oligosaccharide alpha-1,2-mannosidasePRO_0000012085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi182 – 1821N-linked (GlcNAc...)
Disulfide bondi332 ↔ 361
Glycosylationi366 – 3661N-linked (GlcNAc...)
Glycosylationi438 – 4381N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 5822Combined sources
Turni59 – 613Combined sources
Beta strandi62 – 665Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 733Combined sources
Turni75 – 784Combined sources
Helixi81 – 9313Combined sources
Helixi96 – 10813Combined sources
Helixi120 – 13920Combined sources
Turni140 – 1445Combined sources
Helixi149 – 16618Combined sources
Helixi167 – 1704Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi179 – 1813Combined sources
Turni183 – 1853Combined sources
Beta strandi192 – 1954Combined sources
Helixi196 – 2005Combined sources
Helixi203 – 21311Combined sources
Helixi217 – 23014Combined sources
Helixi235 – 2373Combined sources
Beta strandi246 – 2494Combined sources
Turni250 – 2523Combined sources
Turni264 – 2663Combined sources
Helixi267 – 27913Combined sources
Turni281 – 2844Combined sources
Helixi285 – 30117Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi326 – 3283Combined sources
Helixi330 – 3334Combined sources
Helixi334 – 34512Combined sources
Helixi348 – 36619Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi375 – 3784Combined sources
Turni381 – 3833Combined sources
Helixi386 – 3883Combined sources
Helixi389 – 3957Combined sources
Beta strandi398 – 4014Combined sources
Helixi409 – 42113Combined sources
Helixi424 – 44017Combined sources
Beta strandi444 – 4474Combined sources
Helixi456 – 4583Combined sources
Beta strandi459 – 4635Combined sources
Helixi468 – 4714Combined sources
Helixi473 – 4797Combined sources
Beta strandi496 – 4994Combined sources
Beta strandi505 – 5073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31723.
SMRiP31723. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31723.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal

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.

P31723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPVSFPLT VLSLLGSTIA HPYGETEAVL RSEPKSNQAK ADAVKEAFQH
60 70 80 90 100
AWNGYMKYAF PHDELTPVSN GHADSRNGWG ASAVDALSTA VIMGKADVVN
110 120 130 140 150
AILEHVADID FSKTSDTVSL FETTIRYLAG MLSGYDLLQG PAKNLVDNQD
160 170 180 190 200
LIDGLLDQSR NLADVLKFAF DTPSGVPYNN INITSHGNDG ATTNGLAVTG
210 220 230 240 250
TLVLEWTRLS DLTGDEEYAK LSQKAESYLL KPQPSSSEPF PGLVGSSINI
260 270 280 290 300
NDGQFADSRV SWNGGDDSFY EYLIKMYVYD PKRFETYKDR WVLAAESTIK
310 320 330 340 350
HLKSHPKSRP DLTFLSSYSN RNYDLSSQHL TCFDGGSFLL GGTVLDRQDF
360 370 380 390 400
IDFGLELVDG CEATYNSTLT KIGPDSWGWD PKKVPSDQKE FYEKAGFYIS
410 420 430 440 450
SGSYVLRPEV IESFYYAHRV TGKEIYRDWV WNAFVAINST CRTDSGFAAV
460 470 480 490 500
SDVNKANGGS KYDNQESFLF AEVMKYSYLA HSEDAAWQVQ KGGKNTFVYN
510
TEAHPISVAR N
Length:511
Mass (Da):56,570
Last modified:October 1, 1996 - v2
Checksum:iDCBDEBA5768E7596
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti407 – 4071R → H AA sequence (PubMed:8452520).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1.
PIRiS30362.
S58766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1.
PIRiS30362.
S58766.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31723.
SMRiP31723. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.
mycoCLAPiMSD47C1_PENCI.
MSD47C2_PENCI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi3.2.1.113. 4608.

Miscellaneous databases

EvolutionaryTraceiP31723.

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

  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), ACTIVE SITE.

Entry informationi

Entry nameiMAN12_PENCI
AccessioniPrimary (citable) accession number: P31723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.