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A2RB93

- GANA_ASPNC

UniProt

A2RB93 - GANA_ASPNC

Protein

Probable arabinogalactan endo-beta-1,4-galactanase A

Gene

galA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.By similarity

    Catalytic activityi

    The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei152 – 1521Proton donorBy similarity
    Active sitei262 – 2621NucleophileBy similarity

    GO - Molecular functioni

    1. arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB
    2. glucosidase activity Source: InterPro

    GO - Biological processi

    1. pectin catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH53. Glycoside Hydrolase Family 53.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arabinogalactan endo-beta-1,4-galactanase A (EC:3.2.1.89)
    Alternative name(s):
    Endo-1,4-beta-galactanase A
    Short name:
    Galactanase A
    Gene namesi
    Name:galA
    ORF Names:An18g05940
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 8L

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 350334Probable arabinogalactan endo-beta-1,4-galactanase APRO_5000221354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00013963.

    Structurei

    3D structure databases

    ProteinModelPortaliA2RB93.
    SMRiA2RB93. Positions 17-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 53 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000217077.
    OrthoDBiEOG7CG78S.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR011683. Glyco_hydro_53.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07745. Glyco_hydro_53. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2RB93-1 [UniParc]FASTAAdd to Basket

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    MIYSLLLSAL PLLSSAALTY RGADISSLLI EEDAGISYKN LNGETQALED    50
    ILVNNGVNSI RQRVWVDPSD GSYDLDYNLK LAKRVQAAGM SIYLDLHLSD 100
    TWADPSDQTT PTGWSTTDID TLTWQLYNYT LDVCNTFAEN DIDIEIVSIG 150
    NEISSGLLWP LGKTSNYDNI AKLLHSGAWG VKDSNQATTP KIMIHLDNGW 200
    DWEEQEYFYK TVLATGSLLS TDFDLMGVSY YPFYSSEATL SALQTSLTNM 250
    QSNYDKSVVV VETNWPVSCP DPEYSFPSDL SSIPFSAAGQ EEFLEKLAEV 300
    VEGVTDGLGI YYWEPAWVDN AALGSSCADN LMVDIDTDEV LESVTVFEDL 350
    Length:350
    Mass (Da):38,697
    Last modified:March 6, 2007 - v1
    Checksum:i7BB458494EC916FE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270410 Genomic DNA. Translation: CAK43317.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00014232; CADANGAP00013963; CADANGAG00014232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270410 Genomic DNA. Translation: CAK43317.1 .

    3D structure databases

    ProteinModelPortali A2RB93.
    SMRi A2RB93. Positions 17-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00013963.

    Protein family/group databases

    CAZyi GH53. Glycoside Hydrolase Family 53.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00014232 ; CADANGAP00013963 ; CADANGAG00014232 .

    Phylogenomic databases

    HOGENOMi HOG000217077.
    OrthoDBi EOG7CG78S.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR011683. Glyco_hydro_53.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF07745. Glyco_hydro_53. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiGANA_ASPNC
    AccessioniPrimary (citable) accession number: A2RB93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 42 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3