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Q9C4B1

- ABFB_ASPAW

UniProt

Q9C4B1 - ABFB_ASPAW

Protein

Probable alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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
    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. 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.

    Protein family/group databases

    CAZyiCBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPiABF54B_ASPAW.

    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
    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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 499482Probable alpha-L-arabinofuranosidase BPRO_0000394602Add
    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

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C4B1.
    SMRiQ9C4B1. Positions 19-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 335318CatalyticBy 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

    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.

    Q9C4B1-1 [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 ILGIGGYNSN 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):52,646
    Last modified:June 1, 2001 - v1
    Checksum:i839695CA1D57629F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046701 Genomic DNA. Translation: BAB21567.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046701 Genomic DNA. Translation: BAB21567.1 .

    3D structure databases

    ProteinModelPortali Q9C4B1.
    SMRi Q9C4B1. 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_ASPAW.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "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.
      Strain: ATCC 38854 / NBRC 4033.

    Entry informationi

    Entry nameiABFB_ASPAW
    AccessioniPrimary (citable) accession number: Q9C4B1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Lacks the conserved Asp residue in position 297 essential for alpha-L-arabinofuranosidase activity. Its enzyme activity is therefore unsure.Curated

    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