Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q2UIM2

- ABFB_ASPOR

UniProt

Q2UIM2 - ABFB_ASPOR

Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.5. Stable between pH 4.0 and 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    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 sitei426 – 4261Substrate; via amide nitrogenBy similarity
    Binding sitei427 – 4271Substrate; via amide nitrogenBy similarity
    Binding sitei443 – 4431SubstrateBy similarity
    Binding sitei471 – 4711SubstrateBy similarity
    Binding sitei473 – 4731Substrate; via amide nitrogenBy 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.

    Protein family/group databases

    CAZyiCBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPiABF54B_ASPOR.

    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:AO090023000001
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 3

    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 – 506480Alpha-L-arabinofuranosidase BPRO_0000394607Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 39By similarity
    Disulfide bondi89 ↔ 94By similarity
    Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi184 ↔ 185By similarity
    Disulfide bondi409 ↔ 447By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Inductioni

    Repressed by glucose.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00007019.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2UIM2.
    SMRiQ2UIM2. 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.

    Q2UIM2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSGLSLERA CAVALGIVAS ASLVAAGPCD IYSSGGTPCV AAHSTTRALY    50
    SAYTGALYQV KRGSDGSTTD IAPLSAGGVA DAAIQDSFCA NTTCLITIIY 100
    DQSGRGNHLT QAPPGGFNGP ESNGYDNLAS AVGAPVTLNG KKAYGVFMSP 150
    GTGYRNNAAS GTATGDKAEG MYAVLDGTHY NSACCFDYGN AEVSNTDTGN 200
    GHMEAIYYGD NTVWGSGAGS GPWIMADLEN GLFSGLSSTN NAGDPSISYR 250
    FVTAVVKGEA NQWSIRGANA ASGSLSTYYS GARPSASGYN PMSKEGAIIL 300
    GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQADIVAAK YAIASLTSGP 350
    ALTVGSSISL QVTTAGYTTR YLAHDGSTVN TQVVSSSSTT ALRQQASWTV 400
    RTGLANSACL SFESVDTPGS YIRHYNFALL LNANDGTKQF YEDATFCPQA 450
    GLNGQGNSIR SWSYPTRYFR HYENVLYVAS NGGVQTFDAT TSFNDDVSWV 500
    VSTGFA 506
    Length:506
    Mass (Da):52,195
    Last modified:January 24, 2006 - v1
    Checksum:iA0D6B300C19C9420
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461T → A in BAB71804. (PubMed:16233386)Curated
    Sequence conflicti84 – 841I → T in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti167 – 1671K → E in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti387 – 3871S → T in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti390 – 3901T → K in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti393 – 3931R → K in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti410 – 4101L → F in BAB71803. (PubMed:16233386)Curated
    Sequence conflicti429 – 4291L → H in BAB71803. (PubMed:16233386)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB073860 Genomic DNA. Translation: BAB71803.1.
    AB073861 Genomic DNA. Translation: BAB71804.1.
    AP007157 Genomic DNA. Translation: BAE58593.1.
    RefSeqiXP_001820595.1. XM_001820543.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00007157; CADAORAP00007019; CADAORAG00007157.
    GeneIDi5993498.
    KEGGiaor:AOR_1_144.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB073860 Genomic DNA. Translation: BAB71803.1 .
    AB073861 Genomic DNA. Translation: BAB71804.1 .
    AP007157 Genomic DNA. Translation: BAE58593.1 .
    RefSeqi XP_001820595.1. XM_001820543.1.

    3D structure databases

    ProteinModelPortali Q2UIM2.
    SMRi Q2UIM2. Positions 27-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00007019.

    Protein family/group databases

    CAZyi CBM42. Carbohydrate-Binding Module Family 42.
    GH54. Glycoside Hydrolase Family 54.
    mycoCLAPi ABF54B_ASPOR.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00007157 ; CADAORAP00007019 ; CADAORAG00007157 .
    GeneIDi 5993498.
    KEGGi aor:AOR_1_144.

    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. "Synergistic degradation of arabinoxylan with alpha-L-arabinofuranosidase, xylanase and beta-xylosidase from soy sauce koji mold, Aspergillus oryzae, in high salt condition."
      Hashimoto T., Nakata Y.
      J. Biosci. Bioeng. 95:164-169(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 42149 / RIB 40 and HL15.
    2. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiABFB_ASPOR
    AccessioniPrimary (citable) accession number: Q2UIM2
    Secondary accession number(s): Q96VA0, Q96VA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 56 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