SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P31723

- MAN12_PENCI

UniProt

P31723 - MAN12_PENCI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Mannosyl-oligosaccharide alpha-1,2-mannosidase
Gene
MSDC
Organism
Penicillium citrinum
Status
Reviewed - 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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

  1. extracellular region Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35351 Publication
Add
BLAST
Chaini36 – 511476Mannosyl-oligosaccharide alpha-1,2-mannosidase
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP31723.

Family & Domainsi

Sequence similaritiesi

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

MRLPVSFPLT VLSLLGSTIA HPYGETEAVL RSEPKSNQAK ADAVKEAFQH    50
AWNGYMKYAF PHDELTPVSN GHADSRNGWG ASAVDALSTA VIMGKADVVN 100
AILEHVADID FSKTSDTVSL FETTIRYLAG MLSGYDLLQG PAKNLVDNQD 150
LIDGLLDQSR NLADVLKFAF DTPSGVPYNN INITSHGNDG ATTNGLAVTG 200
TLVLEWTRLS DLTGDEEYAK LSQKAESYLL KPQPSSSEPF PGLVGSSINI 250
NDGQFADSRV SWNGGDDSFY EYLIKMYVYD PKRFETYKDR WVLAAESTIK 300
HLKSHPKSRP DLTFLSSYSN RNYDLSSQHL TCFDGGSFLL GGTVLDRQDF 350
IDFGLELVDG CEATYNSTLT KIGPDSWGWD PKKVPSDQKE FYEKAGFYIS 400
SGSYVLRPEV IESFYYAHRV TGKEIYRDWV WNAFVAINST CRTDSGFAAV 450
SDVNKANGGS KYDNQESFLF AEVMKYSYLA HSEDAAWQVQ KGGKNTFVYN 500
TEAHPISVAR N 511
Length:511
Mass (Da):56,570
Last modified:October 1, 1996 - v2
Checksum:iDCBDEBA5768E7596
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti407 – 4071R → H AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1.
PIRiS30362.
S58766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45839 Genomic DNA. Translation: BAA08275.1 .
PIRi S30362.
S58766.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KKT X-ray 2.20 A/B 1-511 [» ]
1KRE X-ray 2.20 A/B 1-511 [» ]
1KRF X-ray 2.20 A/B 1-511 [» ]
2RI8 X-ray 2.16 A/B 36-510 [» ]
2RI9 X-ray 1.95 A/B 36-510 [» ]
ProteinModelPortali P31723.
SMRi P31723. Positions 36-510.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.
mycoCLAPi MSD47C1_PENCI.
MSD47C2_PENCI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

EvolutionaryTracei P31723.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

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).

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: November 13, 2013
This is version 88 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