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Q4WYX7

- ABNA_ASPFU

UniProt

Q4WYX7 - ABNA_ASPFU

Protein

Probable arabinan endo-1,5-alpha-L-arabinosidase A

Gene

abnA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

    Pathwayi

    GO - Molecular functioni

    1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. 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 arabinan endo-1,5-alpha-L-arabinosidase A (EC:3.2.1.99)
    Alternative name(s):
    Endo-1,5-alpha-L-arabinanase A
    Short name:
    ABN A
    Gene namesi
    Name:abnA
    ORF Names:AFUA_3G14620
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 3

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 321302Probable arabinan endo-1,5-alpha-L-arabinosidase APRO_0000394620Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00005003.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WYX7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3507.
    HOGENOMiHOG000292006.
    KOiK06113.
    OMAiGACNVHD.
    OrthoDBiEOG761C4Q.

    Family and domain databases

    Gene3Di2.115.10.20. 1 hit.
    InterProiIPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view]
    PANTHERiPTHR22925. PTHR22925. 1 hit.
    PfamiPF04616. Glyco_hydro_43. 1 hit.
    [Graphical view]
    PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMiSSF75005. SSF75005. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q4WYX7-1 [UniParc]FASTAAdd to Basket

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    MSASVFVVVA SCLAALAHGY ANPGSCLGAC NVHDPALIRR ESDGKYFRFS    50
    TGNKISYASS SSIEGPWTVL GSVLPSGSSI DLPGNDDLWA PDVSLVNGVY 100
    HVYYSVSTFG SQSSAIGLAT SSTMDLNSWT DHGSTGIQSS SSKPYNAIDG 150
    NLFKDGGTYY MNFGSFWHDI YQAPMNSAAT SVASSSYNIA YNPSGTHAVE 200
    GAFMYKYGNY YYLFFSAGIC CGYDTSRPAS GEEYKIKVCR STSATGNFVD 250
    ANGVACTNGG GTVVLESHGN VYGPGGQGVF TDPSLGPILY YHYVDTTIGY 300
    ADSQKLFGWN KIDFSSGWPV V 321
    Length:321
    Mass (Da):34,036
    Last modified:July 5, 2005 - v1
    Checksum:i9D9BFFE699F10574
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000002 Genomic DNA. Translation: EAL92126.1.
    RefSeqiXP_754164.1. XM_749071.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00005003; CADAFUAP00005003; CADAFUAG00005003.
    GeneIDi3512291.
    KEGGiafm:AFUA_3G14620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000002 Genomic DNA. Translation: EAL92126.1 .
    RefSeqi XP_754164.1. XM_749071.1.

    3D structure databases

    ProteinModelPortali Q4WYX7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00005003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00005003 ; CADAFUAP00005003 ; CADAFUAG00005003 .
    GeneIDi 3512291.
    KEGGi afm:AFUA_3G14620.

    Phylogenomic databases

    eggNOGi COG3507.
    HOGENOMi HOG000292006.
    KOi K06113.
    OMAi GACNVHD.
    OrthoDBi EOG761C4Q.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    InterProi IPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view ]
    PANTHERi PTHR22925. PTHR22925. 1 hit.
    Pfami PF04616. Glyco_hydro_43. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMi SSF75005. SSF75005. 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 nameiABNA_ASPFU
    AccessioniPrimary (citable) accession number: Q4WYX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 53 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