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B0XTS5

- ABNB_ASPFC

UniProt

B0XTS5 - ABNB_ASPFC

Protein

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

Gene

abnB

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 34 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arabinan endo-1,5-alpha-L-arabinosidase B (EC:3.2.1.99)
    Alternative name(s):
    Endo-1,5-alpha-L-arabinanase B
    Short name:
    ABN B
    Gene namesi
    Name:abnB
    ORF Names:AFUB_029770
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    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 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 372356Probable arabinan endo-1,5-alpha-L-arabinosidase BPRO_0000394625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliB0XTS5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000292006.
    OrthoDBiEOG761C4Q.
    PhylomeDBiB0XTS5.

    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.

    B0XTS5-1 [UniParc]FASTAAdd to Basket

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    MTVLVALFCL VTWTLCTRIP QYSTQGTQQP QQPEKTPHPH PQPEDAFPPT    50
    HATDLKIHDP SIIHVDGTYY SYSVGRHIRI HQAPSLDGPW ERTGAVLNAD 100
    SVIPKGDRKA PWAPQTVHHN DTYYCFYAVS NSGCRDSAIG VATSKSPGPG 150
    GWTDHGLLVQ SGTGKGSDEH PFTSSNTIDP SVFVGEDGHG YLMFGSFWSG 200
    IWQVPLDESL LSVAGDTSSE ARQLVYMEKA PLPASKHPNP LCREPSGARP 250
    IEGSFLSYHE PWYYLWFSYG KCCKFDTKNL PPPGREYSIR VGRSKSPRGP 300
    FVDKQGRDLA NGGGEIVYAS NRDVYAPGGQ GVLTEKSGDI LYYHYCRYPV 350
    IQEIEVDADL TVNKSTSYDF WV 372
    Length:372
    Mass (Da):41,144
    Last modified:June 15, 2010 - v2
    Checksum:iB031B198AEABB42C
    GO

    Sequence cautioni

    The sequence EDP54917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499595 Genomic DNA. Translation: EDP54917.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499595 Genomic DNA. Translation: EDP54917.1 . Different initiation.

    3D structure databases

    ProteinModelPortali B0XTS5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000292006.
    OrthoDBi EOG761C4Q.
    PhylomeDBi B0XTS5.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiABNB_ASPFC
    AccessioniPrimary (citable) accession number: B0XTS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 34 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

    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