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Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.76 mM for L-arabinofuranose2 Publications

    pH dependencei

    Optimum pH is 4.0. Stable between pH 3.0 and 7.0.2 Publications

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.2 Publications

    Pathwayi: L-arabinan degradation

    This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
    View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei176 – 177Cis-peptide bond1 Publication2
    Binding sitei219Substrate2 Publications1
    Active sitei221Nucleophile1 Publication1
    Binding sitei222Substrate; via amide nitrogen2 Publications1
    Binding sitei223Substrate; via amide nitrogen2 Publications1
    Binding sitei296Substrate; via amide nitrogen2 Publications1
    Active sitei297Proton donor1 Publication1
    Binding sitei416Substrate2 Publications1
    Binding sitei418Substrate; via amide nitrogen2 Publications1
    Binding sitei419Substrate; via amide nitrogen2 Publications1
    Binding sitei435Substrate2 Publications1
    Binding sitei463Substrate2 Publications1
    Binding sitei465Substrate; via amide nitrogen2 Publications1
    Binding sitei468Substrate; via amide nitrogen2 Publications1
    Binding sitei488Substrate2 Publications1

    GO - Molecular functioni

    • alpha-L-arabinofuranosidase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.55. 514.
    SABIO-RKQ8NK89.
    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiCBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPiABF54B_ASPKA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-L-arabinofuranosidase B (EC:3.2.1.55)
    Short name:
    ABF B
    Short name:
    Arabinosidase B
    Gene namesi
    Name:abfB
    ORF Names:AKAW_08685
    OrganismiAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
    Taxonomic identifieri1033177 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    Proteomesi
    • UP000006812 Componenti: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Contribute to an increase in cereal utilization and formation of aroma in shochu brewing.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi176 – 177CC → AA: Decreases the affinity toward the substrate. 1 Publication2
    Mutagenesisi204T → A: Reduces thermostability and catalytic activity. 1 Publication1
    Mutagenesisi221E → A: Impairs catalytic activity. 1 Publication1
    Mutagenesisi297D → A: Impairs catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 17Sequence analysisAdd BLAST17
    ChainiPRO_000039460618 – 499Alpha-L-arabinofuranosidase BAdd BLAST482

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi21 ↔ 311 Publication
    Disulfide bondi81 ↔ 861 Publication
    Glycosylationi83N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi176 ↔ 1771 Publication
    Glycosylationi202N-linked (GlcNAc...)1 Publication1
    Disulfide bondi401 ↔ 4391 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Inductioni

    Expressed in the presence of L-arabitol and L-arabinose, and repressed in the presence of sucrose and glucose.1 Publication

    Structurei

    Secondary structure

    1499
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi20 – 26Combined sources7
    Beta strandi31 – 39Combined sources9
    Beta strandi50 – 54Combined sources5
    Turni55 – 57Combined sources3
    Beta strandi60 – 63Combined sources4
    Beta strandi65 – 67Combined sources3
    Helixi74 – 80Combined sources7
    Turni81 – 83Combined sources3
    Beta strandi86 – 91Combined sources6
    Turni94 – 97Combined sources4
    Beta strandi101 – 103Combined sources3
    Beta strandi107 – 109Combined sources3
    Helixi114 – 116Combined sources3
    Beta strandi121 – 130Combined sources10
    Beta strandi133 – 140Combined sources8
    Beta strandi146 – 150Combined sources5
    Beta strandi161 – 167Combined sources7
    Beta strandi174 – 176Combined sources3
    Beta strandi179 – 183Combined sources5
    Beta strandi196 – 201Combined sources6
    Beta strandi210 – 212Combined sources3
    Beta strandi215 – 219Combined sources5
    Beta strandi224 – 232Combined sources9
    Beta strandi242 – 251Combined sources10
    Beta strandi254 – 261Combined sources8
    Beta strandi264 – 274Combined sources11
    Beta strandi281 – 283Combined sources3
    Beta strandi289 – 294Combined sources6
    Beta strandi304 – 314Combined sources11
    Helixi318 – 331Combined sources14
    Beta strandi333 – 335Combined sources3
    Beta strandi349 – 354Combined sources6
    Beta strandi362 – 367Combined sources6
    Beta strandi370 – 375Combined sources6
    Helixi382 – 387Combined sources6
    Beta strandi390 – 394Combined sources5
    Beta strandi401 – 409Combined sources9
    Beta strandi412 – 417Combined sources6
    Beta strandi420 – 425Combined sources6
    Helixi430 – 435Combined sources6
    Beta strandi438 – 442Combined sources5
    Beta strandi446 – 456Combined sources11
    Beta strandi460 – 464Combined sources5
    Beta strandi467 – 471Combined sources5
    Helixi478 – 480Combined sources3
    Helixi485 – 488Combined sources4
    Beta strandi491 – 495Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WD3X-ray1.75A19-499[»]
    1WD4X-ray2.07A19-499[»]
    2D43X-ray2.80A19-499[»]
    2D44X-ray2.30A19-499[»]
    ProteinModelPortaliQ8NK89.
    SMRiQ8NK89.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NK89.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni18 – 335CatalyticAdd BLAST318
    Regioni336 – 499ABDAdd BLAST164

    Domaini

    Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD).1 Publication

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 54 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    InParanoidiQ8NK89.
    OrthoDBiEOG092C3Z3T.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
    IPR007934. AbfB_ABD.
    IPR013320. ConA-like_dom.
    [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.

    Q8NK89-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY
    60 70 80 90 100
    QLQRGSDDTT TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH
    110 120 130 140 150
    LTQAPPGGFD GPDTDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE
    160 170 180 190 200
    ATGTATGDEA EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL
    210 220 230 240 250
    GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YRFVTAAVKG
    260 270 280 290 300
    GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN
    310 320 330 340 350
    GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV
    360 370 380 390 400
    SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ
    410 420 430 440 450
    CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAALNGEGTS
    460 470 480 490
    LRSWSYPTRY FRHYENVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS
    Length:499
    Mass (Da):52,598
    Last modified:October 1, 2002 - v1
    Checksum:i94B340130BB18746
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB085904 Genomic DNA. Translation: BAB96816.1.
    DF126474 Genomic DNA. Translation: GAA90571.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB085904 Genomic DNA. Translation: BAB96816.1.
    DF126474 Genomic DNA. Translation: GAA90571.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WD3X-ray1.75A19-499[»]
    1WD4X-ray2.07A19-499[»]
    2D43X-ray2.80A19-499[»]
    2D44X-ray2.30A19-499[»]
    ProteinModelPortaliQ8NK89.
    SMRiQ8NK89.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiCBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPiABF54B_ASPKA.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    InParanoidiQ8NK89.
    OrthoDBiEOG092C3Z3T.

    Enzyme and pathway databases

    UniPathwayiUPA00667.
    BRENDAi3.2.1.55. 514.
    SABIO-RKQ8NK89.

    Miscellaneous databases

    EvolutionaryTraceiQ8NK89.

    Family and domain databases

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

    Entry informationi

    Entry nameiABFB_ASPKW
    AccessioniPrimary (citable) accession number: Q8NK89
    Secondary accession number(s): G7XUM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: October 1, 2002
    Last modified: November 2, 2016
    This is version 67 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

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.