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P55296

- MANA_PIRSP

UniProt

P55296 - MANA_PIRSP

Protein

Mannan endo-1,4-beta-mannosidase A

Gene

MANA

Organism
Piromyces sp.
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. Shows very high activity against mannohexaose but not against mannopentaose and smaller mannooligosaccharides. The major products released from mannooligosaccharide hydrolysis are mannose and mannobiose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

    Catalytic activityi

    Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. cellulase activity Source: InterPro
    3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. substituted mannan metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiCBM35. Carbohydrate-Binding Module Family 35.
    GH26. Glycoside Hydrolase Family 26.
    mycoCLAPiMAN26A_PIRSP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
    Alternative name(s):
    1,4-beta-D-mannan mannanohydrolase A
    Beta-mannanase A
    Gene namesi
    Name:MANA
    OrganismiPiromyces sp.
    Taxonomic identifieri45796 [NCBI]
    Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 606587Mannan endo-1,4-beta-mannosidase APRO_0000012174Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP55296.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 140119CBM6PROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 52636CBM10 1Add
    BLAST
    Domaini530 – 56536CBM10 2Add
    BLAST
    Domaini569 – 60436CBM10 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni141 – 471331CatalyticAdd
    BLAST
    Regioni472 – 48918LinkerAdd
    BLAST

    Domaini

    Consists of a catalytic N-terminal domain linked to a reiterated non-catalytic C-terminal domain.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 26 family.Curated
    Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    3.90.1220.10. 3 hits.
    InterProiIPR002883. CBM10/Dockerin_dom.
    IPR005084. CMB_fam6.
    IPR009034. Dockerin_dom_fun.
    IPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR008979. Galactose-bd-like.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02013. CBM_10. 3 hits.
    PF02156. Glyco_hydro_26. 1 hit.
    [Graphical view]
    PRINTSiPR00739. GLHYDRLASE26.
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF64571. SSF64571. 3 hits.
    PROSITEiPS51175. CBM6. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P55296-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSLNVILTL LSLIISVLSK KVYYEAEDGK LNGITVFKEL SGFSGKGYVG    50
    RFENPGNSVT VTVDAPATGM YDLSIIYCAN MGQKINSLTV NDQSVGDITF 100
    TENTKFETKD VGAVYLNKGK NTIGLVSSWG WMWVDAFVIN DAPNAAKDVS 150
    SKLNPTLVNP KAIPAAKKLY DFLKTNYGKR ILSGQVGAAG QAGDEGQEIQ 200
    RIQKATGKLP AVWNMDFIFE SNDCTWRPQN PDITEMAINW WKKYEGKGIM 250
    AAQWHWNIAG KTGDFAFYSK DTTFNLENAV TEGTWEYEKI IKDIDRVSGH 300
    IKKLQAVNMP LIWRPLHENN GDWFWWGNNP KACAKLWKIL YERMVNYHGL 350
    NNLIWLWNGN NDANTPVDYI DIIGVDIYAN DHGPQTTAYN THFDFYGGKK 400
    MVVLSENGRI PDIQQCVDQD VWWGYFQTWN SEFILQDSYH TDAQLKEYFN 450
    HKTVMNMDEL PSFNVDSYNG DSGSSHNGNS ESNSNTGNSD ECWSINLGYP 500
    CCIGDYVVTT DENGDWGVEN NEWCGIVHKS CWSEPLGYPC CVGNTVISAD 550
    ESGDWGVENN EWCGIVHKSC WAEFLGYPCC VGNTVISTDE FGDWGVENDD 600
    WCGILN 606
    Length:606
    Mass (Da):68,055
    Last modified:October 1, 1996 - v1
    Checksum:i79AAFEEFA2725D86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91857 mRNA. Translation: CAA62968.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91857 mRNA. Translation: CAA62968.1 .

    3D structure databases

    ProteinModelPortali P55296.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM35. Carbohydrate-Binding Module Family 35.
    GH26. Glycoside Hydrolase Family 26.
    mycoCLAPi MAN26A_PIRSP.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    3.90.1220.10. 3 hits.
    InterProi IPR002883. CBM10/Dockerin_dom.
    IPR005084. CMB_fam6.
    IPR009034. Dockerin_dom_fun.
    IPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR008979. Galactose-bd-like.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02013. CBM_10. 3 hits.
    PF02156. Glyco_hydro_26. 1 hit.
    [Graphical view ]
    PRINTSi PR00739. GLHYDRLASE26.
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF64571. SSF64571. 3 hits.
    PROSITEi PS51175. CBM6. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
      Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
      J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiMANA_PIRSP
    AccessioniPrimary (citable) accession number: P55296
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3