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Q5BCI8

- MANBA_EMENI

UniProt

Q5BCI8 - MANBA_EMENI

Protein

Beta-mannosidase A

Gene

mndA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    Functioni

    Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei476 – 4761Proton donorBy similarity

    GO - Molecular functioni

    1. beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00280.

    Protein family/group databases

    CAZyiGH2. Glycoside Hydrolase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-mannosidase A (EC:3.2.1.25)
    Alternative name(s):
    Mannanase A
    Short name:
    Mannase A
    Gene namesi
    Name:mndA
    ORF Names:AN1742
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 940919Beta-mannosidase APRO_0000394649Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi15 – 151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi605 – 6051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00008389.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BCI8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3250.
    HOGENOMiHOG000216059.
    KOiK01192.
    OMAiCHATQLF.
    OrthoDBiEOG78D7TH.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR008979. Galactose-bd-like.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00703. Glyco_hydro_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5BCI8-1 [UniParc]FASTAAdd to Basket

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    MHFHGIATQA VLASNITTGS GRHVSLSDVK WTLSSSALNS TVPASLPSQA    50
    HLDLLNAGVI DDPYYGLNEI DLQWIAQANW TYTSDPIPDL LEEYESTWLV 100
    FEGLDTFATV TFCGHNIAST NNQFRQYAFD VSSALKECTG GPVVRIDFAS 150
    APNTVDAIAA DPKTPVWPVQ LTAQLPNRWL MRKQQSDFGW DWGPAFAPCG 200
    PWKPAYVVQL EKTAPIHVLN TDLDIYRQGN INHLPPDQKQ PWVVNASIDF 250
    IGRLPAEPRL LIEIKELETG DVLASQISDS VTLIGTSITG VTTLKDASPK 300
    LWWPSSLGAQ NLYNVTITVF NKTEEVARIT KRTGFRTIFL NQRNITATQL 350
    SQGIAPGANW HFEVNGKEFY AKGSNFIPPD TFWPRVTKQK MTRLLDAVVA 400
    GNQNMLRIWS SGAYLPDFIY DLADERGILL WSEFQFSDSM YPVDEDFLDN 450
    VAQEVVYNVR RVNHHPSLAL WAGGNEIESL MLPLTREADP DNYPKYLAEY 500
    EKLYISLILP LVYENTRSIS YSPSSTTEGY LSVNLSAPVP MTERYENDEP 550
    GAYYGDTDYY NYDTTVSFDY SIYPVGRFAN EFGFHSMPSL QTWQQVADPE 600
    DLYFNSTTVV IHNRHYTSEG YGRIENSSRG MAEMTLGVER YYPIPDNPDS 650
    VANFSAWCLA TQLFQADFYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQG 700
    PTWAGIEYDG RWKVLHYVAR DVYQPIIVSP FWNYTTGDLE IYVTADLWES 750
    AAGTVNLKWL NLSGEQIIDN AGTPTEIPFT VGAINTTKVY STNIHDLNLP 800
    DTRASILTLS LSSQANLPNA AVKTSLTHEN HFTPSFPKDL ELVNPGLELS 850
    YDAHSGIFTV EAKSGVSLYT WLDYPAGLVG YFTENAFLLV PGQKKKVQFV 900
    VQDGPKDQDW EWQSEVTVRS LWDQKSSTFL YALRVATGRP 940
    Length:940
    Mass (Da):105,765
    Last modified:April 26, 2005 - v1
    Checksum:i45E1CBB33D2AFAF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000027 Genomic DNA. Translation: EAA64028.1.
    BN001307 Genomic DNA. Translation: CBF85479.1.
    RefSeqiXP_659346.1. XM_654254.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008389; CADANIAP00008389; CADANIAG00008389.
    GeneIDi2874889.
    KEGGiani:AN1742.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000027 Genomic DNA. Translation: EAA64028.1 .
    BN001307 Genomic DNA. Translation: CBF85479.1 .
    RefSeqi XP_659346.1. XM_654254.1.

    3D structure databases

    ProteinModelPortali Q5BCI8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00008389.

    Protein family/group databases

    CAZyi GH2. Glycoside Hydrolase Family 2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008389 ; CADANIAP00008389 ; CADANIAG00008389 .
    GeneIDi 2874889.
    KEGGi ani:AN1742.2.

    Phylogenomic databases

    eggNOGi COG3250.
    HOGENOMi HOG000216059.
    KOi K01192.
    OMAi CHATQLF.
    OrthoDBi EOG78D7TH.

    Enzyme and pathway databases

    UniPathwayi UPA00280 .

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    2.60.40.320. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR008979. Galactose-bd-like.
    IPR013812. Glyco_hydro_2/20_Ig-like.
    IPR006102. Glyco_hydro_2_Ig-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00703. Glyco_hydro_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49303. SSF49303. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. "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 nameiMANBA_EMENI
    AccessioniPrimary (citable) accession number: Q5BCI8
    Secondary accession number(s): C8VP45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 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