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Q0CEE5

- ABFB_ASPTN

UniProt

Q0CEE5 - ABFB_ASPTN

Protein

Probable alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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
    Sitei184 – 1852Cis-peptide bondBy similarity
    Binding sitei227 – 2271SubstrateBy similarity
    Active sitei229 – 2291NucleophileBy similarity
    Binding sitei230 – 2301Substrate; via amide nitrogenBy similarity
    Binding sitei304 – 3041Substrate; via amide nitrogenBy similarity
    Active sitei305 – 3051Proton donorBy similarity
    Binding sitei424 – 4241SubstrateBy similarity
    Binding sitei427 – 4271Substrate; via amide nitrogenBy similarity
    Binding sitei443 – 4431SubstrateBy similarity
    Binding sitei471 – 4711SubstrateBy similarity
    Binding sitei476 – 4761Substrate; via amide nitrogenBy similarity
    Binding sitei496 – 4961SubstrateBy similarity

    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
    4. 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 alpha-L-arabinofuranosidase B (EC:3.2.1.55)
    Short name:
    ABF B
    Short name:
    Arabinosidase B
    Gene namesi
    Name:abfB
    ORF Names:ATEG_07939
    OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
    Taxonomic identifieri341663 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000007963: Unassembled WGS sequence

    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 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 506480Probable alpha-L-arabinofuranosidase BPRO_0000394608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 39By similarity
    Disulfide bondi89 ↔ 94By similarity
    Disulfide bondi184 ↔ 185By similarity
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi409 ↔ 447By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00002379.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0CEE5.
    SMRiQ0CEE5. Positions 27-506.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 343317CatalyticBy similarityAdd
    BLAST
    Regioni344 – 506163ABDBy 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

    eggNOGiNOG83819.
    HOGENOMiHOG000187007.
    OMAiNIVAAKY.
    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.

    Q0CEE5-1 [UniParc]FASTAAdd to Basket

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    MLLPRGFNRA VVTALGVVGT GTLVAAGPCD IYSSGGTPCV AAHSTTRALY    50
    SAYTGPLYQV KRGSDGATTN IAPLSAGGVA NAAAQDSFCA GTTCLITIIY 100
    DQSGRGNHLT QAPPGGFKGP EANGYDNLAS AIGAPVTLNG QKAYGVFISP 150
    GTGYRNNAAS GTATGDAPEG MYAVLDGTHY NGGCCFDYGN AETSSTDTGN 200
    GHMEAIYFGD NTVWGSGSGS GPWIMADLEN GLFSGSSTKN NAGDPSVSYR 250
    FLTAIVKGKP NQWAIRGANA ASGSLSTYYN GARPNASGYN PMSKEGAIIL 300
    GIGGDNSIGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YAVAPLTSGP 350
    SLTVGSSISL RATTSCCTTR YLAHNGSTVN TQVVSSSSST ALKQQASWTV 400
    RAGLANSACF SFESKDTPGS FIRHYDFVLQ LSANDGTKQF YEDATFCPQS 450
    GLNGQGSSIR SWNYPTRYFR HYNNVLYAAS NGGVHTFDAT GSFNDDVSWV 500
    VSTSFA 506
    Length:506
    Mass (Da):52,197
    Last modified:October 17, 2006 - v1
    Checksum:i10913205A0B91DE1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476604 Genomic DNA. Translation: EAU32201.1.
    RefSeqiXP_001216560.1. XM_001216560.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00002379; CADATEAP00002379; CADATEAG00002379.
    GeneIDi4322793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476604 Genomic DNA. Translation: EAU32201.1 .
    RefSeqi XP_001216560.1. XM_001216560.1.

    3D structure databases

    ProteinModelPortali Q0CEE5.
    SMRi Q0CEE5. Positions 27-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33178.CADATEAP00002379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00002379 ; CADATEAP00002379 ; CADATEAG00002379 .
    GeneIDi 4322793.

    Phylogenomic databases

    eggNOGi NOG83819.
    HOGENOMi HOG000187007.
    OMAi NIVAAKY.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NIH 2624 / FGSC A1156.

    Entry informationi

    Entry nameiABFB_ASPTN
    AccessioniPrimary (citable) accession number: Q0CEE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 43 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