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Q96X54

- ABFA_ASPAW

UniProt

Q96X54 - ABFA_ASPAW

Protein

Probable alpha-L-arabinofuranosidase A

Gene

abfA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

    Pathwayi

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. arabinose metabolic process Source: UniProtKB
    3. L-arabinose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.
    mycoCLAPiABF51A_ASPAW.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable alpha-L-arabinofuranosidase A (EC:3.2.1.55)
    Short name:
    ABF A
    Short name:
    Arabinosidase A
    Gene namesi
    Name:abfA
    OrganismiAspergillus awamori (Black koji mold)
    Taxonomic identifieri105351 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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 – 25251 PublicationAdd
    BLAST
    Chaini26 – 628603Probable alpha-L-arabinofuranosidase APRO_0000394596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ96X54.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR010720. Alpha-L-AF_C.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SMARTiSM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q96X54-1 [UniParc]FASTAAdd to Basket

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    MVAFSALSGV SALSLLLCLV QHAHGVSLKV STQGGNSSSP ILYGFMFEDI    50
    NHSGDGGIYG QLLQNPGLQG TTPNLTAWAA VGDATIAIDG DSPLTSAIPS 100
    TIKLDVADDA TGAVGLTNEG YWGIPVDGSE FQSSFWIKGD YSGDITVRLV 150
    GNYTGTEYGS ATITHTSTAD NFTQASVKFP TTKAPDGNVL YELTVDGSVA 200
    AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLADMKGSFL RFPGGNNLEG 250
    NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP 300
    VLGVWDGFAL ESGGNTPITG DALTPYIDDV LNELEYILGD TSTTYGAWRA 350
    ANGQEEPWNL TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA 400
    STSEADCLPE SMPEGSWVDY HDYSTPDGLV GQFNYFDNLY RSVPYFIGEY 450
    SRWEIDWPNM KGSVSEAVFM IGFERNSDVV KMAAYAPLLQ LVNSTQWTPD 500
    LIGYTQSPDD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF GPLYWVASSA 550
    GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADNDPDA YNSDTQTLVT 600
    PSESTVQASN GTFTFSLPAW AVAVLAAN 628
    Length:628
    Mass (Da):68,007
    Last modified:December 1, 2001 - v1
    Checksum:i84E4AF25C4805BE4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046702 Genomic DNA. Translation: BAB21568.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046702 Genomic DNA. Translation: BAB21568.2 .

    3D structure databases

    ProteinModelPortali Q96X54.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.
    mycoCLAPi ABF51A_ASPAW.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    InterProi IPR010720. Alpha-L-AF_C.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SMARTi SM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori."
      Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I., Matsuzawa H.
      J. Biosci. Bioeng. 96:232-241(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-43.
      Strain: ATCC 38854 / NBRC 4033.

    Entry informationi

    Entry nameiABFA_ASPAW
    AccessioniPrimary (citable) accession number: Q96X54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 45 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

    Direct protein sequencing

    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