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Q5BF93

- MNS1B_EMENI

UniProt

Q5BF93 - MNS1B_EMENI

Protein

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

Gene

mns1B

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Ca2+. Can also use Mg2+, but with lower efficiency By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei368 – 3681Proton donorBy similarity

    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

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:mns1B
    Synonyms:msdS
    ORF Names:AN0787
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VIII

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle lumen Source: UniProtKB-SubCell
    2. membrane Source: InterPro

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 505489Mannosyl-oligosaccharide alpha-1,2-mannosidase 1BPRO_0000394823Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi325 ↔ 354By similarity
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00001876.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BF93.
    SMRiQ5BF93. Positions 30-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181987.
    KOiK01230.
    OMAiYAFPHDS.
    OrthoDBiEOG7BP8BH.

    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.

    Q5BF93-1 [UniParc]FASTAAdd to Basket

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    MRTLLALAAL AGFAAARVPA YAITRPVMRS DSRADAVKEA FSHAWDGYYN    50
    YAFPHDELHP ISNGYGDSRN HWGASAVDAL STAIMMRNAT IVNQILDHIA 100
    AVDYSKTNAM VSLFETTIRY LAGMISGYDL LKGPAAGLVD DSRVDVLLEQ 150
    SQNLAEVLKF AFDTPSGVPY NMINITSGGN DGATTNGLAV TGTLVLEWTR 200
    LSDLTGNDEY ARLSQRAEDY LLHPEPAQYE PFPGLIGSAV NIADGKLANG 250
    HISWNGGADS YYEYLIKMYV YDPERFGLYR DRWVAAAESS INHLASHPST 300
    RPDVTFLATY NEEHQLGLTS QHLTCFDGGS FLLGGTLLDR QDFVDFGLDL 350
    VAGCHETYNS TLTGIGPEQF SWDPNGVPDS QKELFERAGF YINSGQYILR 400
    PEVIESFYYA WRVTGDGTYR EWVWNAFTNI NKYCRTATGF AGLENVNAAN 450
    GGGRIDNQES FMFAEVLKYS FLTFAPEDDW QVQKGSGNTF VYNTEAHPFK 500
    VYTPQ 505
    Length:505
    Mass (Da):55,881
    Last modified:June 15, 2010 - v2
    Checksum:iEC77168E8C363B6F
    GO

    Sequence cautioni

    The sequence EAA65617.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101L → F in AAG48159. (PubMed:10974561)Curated
    Sequence conflicti420 – 4201R → L in AAG48159. (PubMed:10974561)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129496 Genomic DNA. Translation: AAG48159.1.
    DQ490469 mRNA. Translation: ABF50845.1.
    AACD01000013 Genomic DNA. Translation: EAA65617.1. Sequence problems.
    BN001308 Genomic DNA. Translation: CBF88785.1.
    RefSeqiXP_658391.1. XM_653299.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00001876; CADANIAP00001876; CADANIAG00001876.
    GeneIDi2876566.
    KEGGiani:AN0787.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129496 Genomic DNA. Translation: AAG48159.1 .
    DQ490469 mRNA. Translation: ABF50845.1 .
    AACD01000013 Genomic DNA. Translation: EAA65617.1 . Sequence problems.
    BN001308 Genomic DNA. Translation: CBF88785.1 .
    RefSeqi XP_658391.1. XM_653299.1.

    3D structure databases

    ProteinModelPortali Q5BF93.
    SMRi Q5BF93. Positions 30-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00001876.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00001876 ; CADANIAP00001876 ; CADANIAG00001876 .
    GeneIDi 2876566.
    KEGGi ani:AN0787.2.

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181987.
    KOi K01230.
    OMAi YAFPHDS.
    OrthoDBi EOG7BP8BH.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    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. "Characterization of the class I alpha-mannosidase gene family in the filamentous fungus Aspergillus nidulans."
      Eades C.J., Hintz W.E.
      Gene 255:25-34(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: SM222.
    2. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiMNS1B_EMENI
    AccessioniPrimary (citable) accession number: Q5BF93
    Secondary accession number(s): C8VQU4, Q1HFV5, Q9HF85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 55 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3