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Q5B8T6

- ABND_EMENI

UniProt

Q5B8T6 - ABND_EMENI

Protein

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

Gene

abnD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      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.

    Protein family/group databases

    CAZyiGH43. Glycoside Hydrolase Family 43.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arabinan endo-1,5-alpha-L-arabinosidase D (EC:3.2.1.99)
    Alternative name(s):
    Endo-1,5-alpha-L-arabinanase D
    Short name:
    ABN D
    Gene namesi
    Name:abnD
    ORF Names:AN3044
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VI

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 356334Probable arabinan endo-1,5-alpha-L-arabinosidase DPRO_0000394640Add
    BLAST
    Propeptidei357 – 38327Removed in mature formSequence AnalysisPRO_0000394641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Lipidationi356 – 3561GPI-anchor amidated asparagineSequence Analysis

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00010035.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B8T6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3507.
    HOGENOMiHOG000292006.
    KOiK06113.
    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.

    Q5B8T6-1 [UniParc]FASTAAdd to Basket

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    MVHITLPGLL LCLCLYLSVA PANPLNAHAR VSDTTAFPLP NEGHVVAHDP    50
    SIVRHHEHFY LFKGGIHIPV FRASNLSGPW ERLGTVLNGP SLVQKQNQRR 100
    PWAPMVTQWK NRFYCFYSIS QNGKRNSAIG VASSDSVEPG GWTDHGPLIN 150
    TGHGPGSGVY PFNVSNAIDP AFFADPITGQ PYLQYGSYWK GIFQVPLAED 200
    LLSVENATHP NTDHLVFLPK KKPKPNEGVF MSYRAPYYYA WFSHGQCCHF 250
    KTQGFPKEGN EYSIRVGRST SVHGPFVDRD NKDLLNGGGS VVYGSNHGKV 300
    YAPGGLGVLP GANGEPDVLY YHYHNASIGF AQGDARLGWN YLDYVDGWPV 350
    PRAPSNPGNS LQPPSSVSLQ IVAFLCLVIL FTL 383
    Length:383
    Mass (Da):42,055
    Last modified:June 15, 2010 - v2
    Checksum:i32573F128157AE8A
    GO

    Sequence cautioni

    The sequence CBF83510.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAA63615.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490482 mRNA. Translation: ABF50858.1.
    AACD01000051 Genomic DNA. Translation: EAA63615.1. Sequence problems.
    BN001306 Genomic DNA. Translation: CBF83510.1. Sequence problems.
    RefSeqiXP_660648.1. XM_655556.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00010035; CADANIAP00010035; CADANIAG00010035.
    GeneIDi2873991.
    KEGGiani:AN3044.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490482 mRNA. Translation: ABF50858.1 .
    AACD01000051 Genomic DNA. Translation: EAA63615.1 . Sequence problems.
    BN001306 Genomic DNA. Translation: CBF83510.1 . Sequence problems.
    RefSeqi XP_660648.1. XM_655556.1.

    3D structure databases

    ProteinModelPortali Q5B8T6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00010035.

    Protein family/group databases

    CAZyi GH43. Glycoside Hydrolase Family 43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00010035 ; CADANIAP00010035 ; CADANIAG00010035 .
    GeneIDi 2873991.
    KEGGi ani:AN3044.2.

    Phylogenomic databases

    eggNOGi COG3507.
    HOGENOMi HOG000292006.
    KOi K06113.
    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. "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: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    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.

    Entry informationi

    Entry nameiABND_EMENI
    AccessioniPrimary (citable) accession number: Q5B8T6
    Secondary accession number(s): C8VIS9, Q1HFU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 52 of the entry and version 2 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