Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P31723

- MAN12_PENCI

UniProt

P31723 - MAN12_PENCI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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 – 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.
    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

    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

    Experimental Info

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

    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: October 1, 2014
    This is version 89 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