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O74288

- ABFB_EMENI

UniProt

O74288 - ABFB_EMENI

Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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.

    pH dependencei

    Optimum pH is 4.8.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei182 – 1832Cis-peptide bondBy similarity
    Binding sitei225 – 2251SubstrateBy similarity
    Active sitei227 – 2271NucleophileBy similarity
    Binding sitei228 – 2281Substrate; via amide nitrogenBy similarity
    Binding sitei303 – 3031Substrate; via amide nitrogenBy similarity
    Active sitei304 – 3041Proton donorBy similarity
    Binding sitei427 – 4271SubstrateBy similarity
    Binding sitei429 – 4291Substrate; via amide nitrogenBy similarity
    Binding sitei430 – 4301Substrate; via amide nitrogenBy similarity
    Binding sitei446 – 4461SubstrateBy similarity
    Binding sitei475 – 4751SubstrateBy similarity
    Binding sitei477 – 4771Substrate; via amide nitrogenBy similarity
    Binding sitei480 – 4801Substrate; via amide nitrogenBy similarity
    Binding sitei500 – 5001SubstrateBy 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. pectin catabolic process Source: UniProtKB
    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.
    mycoCLAPiABF54B_EMENI.

    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:AN1571
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 510486Alpha-L-arabinofuranosidase BPRO_0000394609Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 37By similarity
    Disulfide bondi87 ↔ 92By similarity
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi182 ↔ 183By similarity
    Disulfide bondi412 ↔ 450By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Inductioni

    Expressed in presence of L-arabinol and repressed in presence of glucose and glycerol. Expression is also pH regulated probably through the action of the pacC transcription factor and is higher at acidic pHs.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00008202.

    Structurei

    3D structure databases

    ProteinModelPortaliO74288.
    SMRiO74288. Positions 25-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 342318CatalyticBy similarityAdd
    BLAST
    Regioni343 – 510168ABDBy 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.

    O74288-1 [UniParc]FASTAAdd to Basket

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    MTMSRSSRSS VLALALATGS LVAAGPCDIY SSGGTPCIAA HSTTRALYSS    50
    YNGPLYQVQR ASDGTTTTIT PLSAGGVADA SAQDAFCENT TCLITIIYDQ 100
    SGNGNDLTQA PPGGFNGPDV GGYDNLAGAI GAPVTLNGKK AYGVFVSPGT 150
    GYRNNEAIGT ATGDEPEGMY AVLDGTHYND GCCFDYGNAE TSSLDTGNGH 200
    MEAIYYGTNT AWGYGAGNGP WIMADLENGL FSGQSSDYNA GDPSISYRFV 250
    TAILKGGPNL WALRGGNAAS GSLSTYYNGI RPTDASGYNP MSKEGAIILG 300
    IGGDNSVSAQ GTFYEGAMTD GYPDDATENS VQADIVAAKY ATTSLISGPA 350
    LTVGDTVSLK VTTSGYDTRY IAHTGSTINT QVVSSSSSST LKQQASWTVR 400
    TGLASTAAAN GCVSFESVDT PGSYIRHSNF ALLLNANDGT KLFSEDATFC 450
    PQDSFNDDGT NSIRSWNYPT RYWRHYENVL YVASNGGVNT FDAATAFTDD 500
    VSWVVADGFA 510
    Length:510
    Mass (Da):52,942
    Last modified:November 1, 1998 - v1
    Checksum:i54011DA6AD3BFC22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13759 Genomic DNA. Translation: CAA74084.1.
    AACD01000025 Genomic DNA. Translation: EAA64278.1.
    BN001307 Genomic DNA. Translation: CBF85134.1.
    RefSeqiXP_659175.1. XM_654083.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008202; CADANIAP00008202; CADANIAG00008202.
    GeneIDi2875522.
    KEGGiani:AN1571.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13759 Genomic DNA. Translation: CAA74084.1 .
    AACD01000025 Genomic DNA. Translation: EAA64278.1 .
    BN001307 Genomic DNA. Translation: CBF85134.1 .
    RefSeqi XP_659175.1. XM_654083.1.

    3D structure databases

    ProteinModelPortali O74288.
    SMRi O74288. Positions 25-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00008202.

    Protein family/group databases

    CAZyi CBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPi ABF54B_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008202 ; CADANIAP00008202 ; CADANIAG00008202 .
    GeneIDi 2875522.
    KEGGi ani:AN1571.2.

    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. "The abfB gene encoding the major alpha-L-arabinofuranosidase of Aspergillus nidulans: nucleotide sequence, regulation and construction of a disrupted strain."
      Gielkens M., Gonzalez-Candelas L., Sanchez-Torres P., van de Vondervoort P., de Graaff L., Visser J., Ramon D.
      Microbiology 145:735-741(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, FUNCTION.
      Strain: ArgB2, biA1 and MetG1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiABFB_EMENI
    AccessioniPrimary (citable) accession number: O74288
    Secondary accession number(s): C8VN12, Q5BD09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 71 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