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)

Q4WL66

- ABFB_ASPFU

UniProt

Q4WL66 - ABFB_ASPFU

Protein

Probable alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      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 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
    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 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.

    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
    ORF Names:AFUA_6G14620
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 6

    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 – 506480Probable alpha-L-arabinofuranosidase BPRO_0000394605Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 39By similarity
    Disulfide bondi89 ↔ 94By similarity
    Disulfide bondi184 ↔ 185By similarity
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi409 ↔ 447By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00002338.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WL66.
    SMRiQ4WL66. 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.

    Q4WL66-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPQLSIERA SVFALGLIAT GSLVVAGPCD IYSAGGTPCV AAHSTTRALY    50
    SSYSGPLYQV KRGSDGATAD IAPLSAGGVA NAAAQDSFCD GTTCLITIIY 100
    DQSGRGNHLT QAPPGGFSGP ESNGYDNLAS AIGAPVTLNG QKAYGVFISP 150
    GTGYRNNAAS GTATGDAPEG MYAVLDGTHY NDACCFDYGN AETSSRDTGN 200
    GHMEAIYFGD NTIWGTGSGS GPWIMADLEN GLFSGSSPDN NSGDPSISYR 250
    FLTAVVKGKQ NQWAIRGANA ASGSLSTFYN GARPSVSGYN PMSKEGAIIL 300
    GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YATASLTSGP 350
    KLTVGSSISL QATTPGYTTR YIAHSGSTVN TQVVSSSSST TLKQQASWTV 400
    RTGLANSDCF SFESRDTPGS FLRHYNFVLQ LSANDGTKQF HEDATFCPQA 450
    GLNGQGNSIR SWNYPTRYFR HYNNVLYAAS NGGVHTFDAT SSFNNDVSWV 500
    ISTGFA 506
    Length:506
    Mass (Da):52,548
    Last modified:July 5, 2005 - v1
    Checksum:i7EE4CD1C4B1A3224
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL89298.1.
    RefSeqiXP_751336.1. XM_746243.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00002338; CADAFUAP00002338; CADAFUAG00002338.
    GeneIDi3508653.
    KEGGiafm:AFUA_6G14620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000006 Genomic DNA. Translation: EAL89298.1 .
    RefSeqi XP_751336.1. XM_746243.1.

    3D structure databases

    ProteinModelPortali Q4WL66.
    SMRi Q4WL66. Positions 27-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00002338.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00002338 ; CADAFUAP00002338 ; CADAFUAG00002338 .
    GeneIDi 3508653.
    KEGGi afm:AFUA_6G14620.

    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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiABFB_ASPFU
    AccessioniPrimary (citable) accession number: Q4WL66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    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

    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