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A5AAG2

- ABNC_ASPNC

UniProt

A5AAG2 - ABNC_ASPNC

Protein

Probable arabinan endo-1,5-alpha-L-arabinosidase C

Gene

abnC

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 40 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
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    Functioni

    Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

    Pathwayi

    GO - Molecular functioni

    1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH43. Glycoside Hydrolase Family 43.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arabinan endo-1,5-alpha-L-arabinosidase C (EC:3.2.1.99)
    Alternative name(s):
    Endo-1,5-alpha-L-arabinanase C
    Short name:
    ABN C
    Gene namesi
    Name:abnC
    ORF Names:An02g10550
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 4R

    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 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 318290Probable arabinan endo-1,5-alpha-L-arabinosidase CPRO_5000242344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00002504.

    Structurei

    3D structure databases

    ProteinModelPortaliA5AAG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3507.
    HOGENOMiHOG000292006.
    KOiK06113.
    OrthoDBiEOG761C4Q.

    Family and domain databases

    Gene3Di2.115.10.20. 1 hit.
    InterProiIPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view]
    PANTHERiPTHR22925. PTHR22925. 1 hit.
    PfamiPF04616. Glyco_hydro_43. 1 hit.
    [Graphical view]
    PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMiSSF75005. SSF75005. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A5AAG2-1 [UniParc]FASTAAdd to Basket

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    MLSFVLLLCV ALVNAYSDPG ACSGTCWAHD PNVIRRVSDG TYFRFSTGGG    50
    VHISSASAIT GPWTDLGYAL PNGSIVTVGN ASNLWAPDVH YVDGTYYMYY 100
    ASSTLGSRDS TIGVATSTTL EADSWTDHGE IGVTSSSSTP YNAIDPNWIT 150
    IGSTPYLQFG SYWQGLYQVE MTDSLSASSS TPTNLAYNAS GNHAIEASYL 200
    YEYGGYYYLT FSSGKAQGYT TSLPAQGDEY RIVVCRSKTG TGNFVDKDGV 250
    SCLNSGGTTV LASHDYVYGP GGQGIINTTS HGIVVYYHYA NKNIGLAVDD 300
    YQFGWNTLTW TDGWPVVA 318
    Length:318
    Mass (Da):34,047
    Last modified:June 12, 2007 - v1
    Checksum:iE90B7BEBFF22EEE3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270026 Genomic DNA. Translation: CAK44404.1.
    RefSeqiXP_001400184.1. XM_001400147.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00002573; CADANGAP00002504; CADANGAG00002573.
    GeneIDi4979546.
    KEGGiang:ANI_1_1480024.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270026 Genomic DNA. Translation: CAK44404.1 .
    RefSeqi XP_001400184.1. XM_001400147.2.

    3D structure databases

    ProteinModelPortali A5AAG2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00002504.

    Protein family/group databases

    CAZyi GH43. Glycoside Hydrolase Family 43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00002573 ; CADANGAP00002504 ; CADANGAG00002573 .
    GeneIDi 4979546.
    KEGGi ang:ANI_1_1480024.

    Phylogenomic databases

    eggNOGi COG3507.
    HOGENOMi HOG000292006.
    KOi K06113.
    OrthoDBi EOG761C4Q.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    InterProi IPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view ]
    PANTHERi PTHR22925. PTHR22925. 1 hit.
    Pfami PF04616. Glyco_hydro_43. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMi SSF75005. SSF75005. 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 nameiABNC_ASPNC
    AccessioniPrimary (citable) accession number: A5AAG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 40 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