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A2R511

- ABFB_ASPNC

UniProt

A2R511 - ABFB_ASPNC

Protein

Probable alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei176 – 1772Cis-peptide bondBy similarity
    Binding sitei219 – 2191SubstrateBy similarity
    Active sitei221 – 2211NucleophileBy similarity
    Binding sitei222 – 2221Substrate; via amide nitrogenBy similarity
    Binding sitei223 – 2231Substrate; via amide nitrogenBy similarity
    Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
    Active sitei297 – 2971Proton donorBy similarity
    Binding sitei416 – 4161SubstrateBy similarity
    Binding sitei418 – 4181Substrate; via amide nitrogenBy similarity
    Binding sitei419 – 4191Substrate; via amide nitrogenBy similarity
    Binding sitei435 – 4351SubstrateBy similarity
    Binding sitei463 – 4631SubstrateBy similarity
    Binding sitei465 – 4651Substrate; via amide nitrogenBy similarity
    Binding sitei468 – 4681Substrate; via amide nitrogenBy similarity
    Binding sitei488 – 4881SubstrateBy similarity

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. arabinan metabolic process Source: ASPGD
    3. arabinose metabolic process Source: UniProtKB
    4. L-arabinose metabolic process Source: InterPro
    5. 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

    CAZyiCBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable alpha-L-arabinofuranosidase B (EC:3.2.1.55)
    Short name:
    ABF B
    Short name:
    Arabinosidase B
    Gene namesi
    Name:abfB
    ORF Names:An15g02300
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 3R

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. intracellular Source: ASPGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 499481Probable alpha-L-arabinofuranosidase BPRO_5000221024Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 31By similarity
    Disulfide bondi81 ↔ 86By similarity
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi176 ↔ 177By similarity
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi401 ↔ 439By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00011686.

    Structurei

    3D structure databases

    ProteinModelPortaliA2R511.
    SMRiA2R511. Positions 19-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 335317CatalyticBy similarityAdd
    BLAST
    Regioni336 – 499164ABDBy similarityAdd
    BLAST

    Domaini

    Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD).By similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 54 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000187007.
    OrthoDBiEOG7DFXNQ.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
    IPR007934. AbfB.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [Graphical view]
    PfamiPF05270. AbfB. 1 hit.
    PF09206. ArabFuran-catal. 1 hit.
    [Graphical view]
    SUPFAMiSSF110221. SSF110221. 1 hit.
    SSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2R511-1 [UniParc]FASTAAdd to Basket

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    MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY    50
    QLQRGSDDTT TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH 100
    LTQAPPGGFD GPDVDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE 150
    ATGTATGDEP EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL 200
    GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YSFVTAAVKG 250
    GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 300
    GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV 350
    SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ 400
    CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAPLNGEGTS 450
    LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS 499
    Length:499
    Mass (Da):52,509
    Last modified:March 6, 2007 - v1
    Checksum:iF1F6C21F601419C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270337 Genomic DNA. Translation: CAK42333.1.
    RefSeqiXP_001396769.1. XM_001396732.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00011909; CADANGAP00011686; CADANGAG00011909.
    GeneIDi4987831.
    KEGGiang:ANI_1_372134.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270337 Genomic DNA. Translation: CAK42333.1 .
    RefSeqi XP_001396769.1. XM_001396732.2.

    3D structure databases

    ProteinModelPortali A2R511.
    SMRi A2R511. Positions 19-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00011686.

    Protein family/group databases

    CAZyi CBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00011909 ; CADANGAP00011686 ; CADANGAG00011909 .
    GeneIDi 4987831.
    KEGGi ang:ANI_1_372134.

    Phylogenomic databases

    HOGENOMi HOG000187007.
    OrthoDBi EOG7DFXNQ.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR015289. A-L-arabinofuranosidase_B_cat.
    IPR007934. AbfB.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [Graphical view ]
    Pfami PF05270. AbfB. 1 hit.
    PF09206. ArabFuran-catal. 1 hit.
    [Graphical view ]
    SUPFAMi SSF110221. SSF110221. 1 hit.
    SSF49899. SSF49899. 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 nameiABFB_ASPNC
    AccessioniPrimary (citable) accession number: A2R511
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 52 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