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Q8NK89

- ABFB_ASPKW

UniProt

Q8NK89 - ABFB_ASPKW

Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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.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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei176 – 1772Cis-peptide bond
    Binding sitei219 – 2191Substrate2 Publications
    Active sitei221 – 2211Nucleophile1 Publication
    Binding sitei222 – 2221Substrate; via amide nitrogen2 Publications
    Binding sitei223 – 2231Substrate; via amide nitrogen2 Publications
    Binding sitei296 – 2961Substrate; via amide nitrogen2 Publications
    Active sitei297 – 2971Proton donor1 Publication
    Binding sitei416 – 4161Substrate2 Publications
    Binding sitei418 – 4181Substrate; via amide nitrogen2 Publications
    Binding sitei419 – 4191Substrate; via amide nitrogen2 Publications
    Binding sitei435 – 4351Substrate2 Publications
    Binding sitei463 – 4631Substrate2 Publications
    Binding sitei465 – 4651Substrate; via amide nitrogen2 Publications
    Binding sitei468 – 4681Substrate; via amide nitrogen2 Publications
    Binding sitei488 – 4881Substrate2 Publications

    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

    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
    ProteomesiUP000006812: Unassembled WGS sequence

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1772CC → AA: Decreases the affinity toward the substrate.
    Mutagenesisi204 – 2041T → A: Reduces thermostability and catalytic activity. 1 Publication
    Mutagenesisi221 – 2211E → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi297 – 2971D → A: Impairs catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 499482Alpha-L-arabinofuranosidase BPRO_0000394606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 311 Publication
    Disulfide bondi81 ↔ 861 Publication
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi176 ↔ 1771 Publication
    Glycosylationi202 – 2021N-linked (GlcNAc...)1 Publication
    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

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 267
    Beta strandi31 – 399
    Beta strandi50 – 545
    Turni55 – 573
    Beta strandi60 – 634
    Beta strandi65 – 673
    Helixi74 – 807
    Turni81 – 833
    Beta strandi86 – 916
    Turni94 – 974
    Beta strandi101 – 1033
    Beta strandi107 – 1093
    Helixi114 – 1163
    Beta strandi121 – 13010
    Beta strandi133 – 1408
    Beta strandi146 – 1505
    Beta strandi161 – 1677
    Beta strandi174 – 1763
    Beta strandi179 – 1835
    Beta strandi196 – 2016
    Beta strandi210 – 2123
    Beta strandi215 – 2195
    Beta strandi224 – 2329
    Beta strandi242 – 25110
    Beta strandi254 – 2618
    Beta strandi264 – 27411
    Beta strandi281 – 2833
    Beta strandi289 – 2946
    Beta strandi304 – 31411
    Helixi318 – 33114
    Beta strandi333 – 3353
    Beta strandi349 – 3546
    Beta strandi362 – 3676
    Beta strandi370 – 3756
    Helixi382 – 3876
    Beta strandi390 – 3945
    Beta strandi401 – 4099
    Beta strandi412 – 4176
    Beta strandi420 – 4256
    Helixi430 – 4356
    Beta strandi438 – 4425
    Beta strandi446 – 45611
    Beta strandi460 – 4645
    Beta strandi467 – 4715
    Helixi478 – 4803
    Helixi485 – 4884
    Beta strandi491 – 4955

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WD3X-ray1.75A19-499[»]
    1WD4X-ray2.07A19-499[»]
    2D43X-ray2.80A19-499[»]
    2D44X-ray2.30A19-499[»]
    ProteinModelPortaliQ8NK89.
    SMRiQ8NK89. Positions 19-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NK89.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 335318CatalyticAdd
    BLAST
    Regioni336 – 499164ABDAdd
    BLAST

    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

    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.

    Q8NK89-1 [UniParc]FASTAAdd to Basket

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    MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY    50
    QLQRGSDDTT TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH 100
    LTQAPPGGFD GPDTDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE 150
    ATGTATGDEA EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL 200
    GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YRFVTAAVKG 250
    GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 300
    GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV 350
    SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ 400
    CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAALNGEGTS 450
    LRSWSYPTRY FRHYENVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS 499
    Length:499
    Mass (Da):52,598
    Last modified:October 1, 2002 - v1
    Checksum:i94B340130BB18746
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB085904 Genomic DNA. Translation: BAB96816.1.
    DF126474 Genomic DNA. Translation: GAA90571.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB085904 Genomic DNA. Translation: BAB96816.1 .
    DF126474 Genomic DNA. Translation: GAA90571.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WD3 X-ray 1.75 A 19-499 [» ]
    1WD4 X-ray 2.07 A 19-499 [» ]
    2D43 X-ray 2.80 A 19-499 [» ]
    2D44 X-ray 2.30 A 19-499 [» ]
    ProteinModelPortali Q8NK89.
    SMRi Q8NK89. Positions 19-499.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPi ABF54B_ASPKA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG7DFXNQ.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .
    SABIO-RK Q8NK89.

    Miscellaneous databases

    EvolutionaryTracei Q8NK89.

    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. "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 18-27 AND 421-432, SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
      Strain: NBRC 4308.
    2. "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
      Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
      Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NBRC 4308.
    3. "Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."
      Miyanaga A., Koseki T., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
      J. Biol. Chem. 279:44907-44914(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 19-499 IN COMPLEX WITH SUBSTRATE, DOMAIN, ACTIVE SITE, DISULFIDE BONDS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-202, MUTAGENESIS OF 176-CYS-CYS-177; THR-204; GLU-221 AND ASP-297.
      Strain: NBRC 4308.
    4. "The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose."
      Miyanaga A., Koseki T., Miwa Y., Mese Y., Nakamura S., Kuno A., Hirabayashi J., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
      Biochem. J. 399:503-511(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-499 OF THE ALA-221 MUTANT IN COMPLEX WITH SUBSTRATE.
      Strain: NBRC 4308.

    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: October 1, 2014
    This is version 55 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

    External Data

    Dasty 3