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)

P82594

- IABF_STRCX

UniProt

P82594 - IABF_STRCX

Protein

Extracellular exo-alpha-(1->5)-L-arabinofuranosidase

Gene
N/A
Organism
Streptomyces chartreusis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes only the cleavage of terminal alpha-(1->5) arabinofuranosyl bonds of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing polysaccharides and arabinoxylo-oligosaccharides.1 Publication

    Catalytic activityi

    Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.1 Publication

    pH dependencei

    Optimum pH is 7.0. The enzyme is slowly inactivated above pH 9 and below pH 5.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. The enzyme is inactivated at temperatures above 40 degrees Celsius.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH43. Glycoside Hydrolase Family 43.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular exo-alpha-(1->5)-L-arabinofuranosidase (EC:3.2.1.55)
    Short name:
    ABF
    Alternative name(s):
    Alpha-L-AFase
    Extracellular arabinan exo-alpha-(1->5)-L-arabinosidase
    Short name:
    Arabinosidase
    OrganismiStreptomyces chartreusis
    Taxonomic identifieri1969 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    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 – 4343Tat-tyPE signal1 PublicationAdd
    BLAST
    Chaini44 – 328285Extracellular exo-alpha-(1->5)-L-arabinofuranosidasePRO_0000012203Add
    BLAST

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

    Structurei

    3D structure databases

    ProteinModelPortaliP82594.
    SMRiP82594. Positions 51-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.115.10.20. 1 hit.
    InterProiIPR016828. Alpha-L-arabinofuranosidase.
    IPR006710. Glyco_hydro_43.
    IPR023296. Glyco_hydro_beta-prop.
    IPR006311. TAT_signal.
    [Graphical view]
    PANTHERiPTHR22925. PTHR22925. 1 hit.
    PfamiPF04616. Glyco_hydro_43. 1 hit.
    [Graphical view]
    PIRSFiPIRSF025414. Alpha-L-arabinofuranosidase. 1 hit.
    SUPFAMiSSF75005. SSF75005. 1 hit.
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P82594-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCTREAVRMS REHDLPEIPS RRLLLKGAAA AGALTAVPGV AHAAPRPAPY    50
    ENPLVRQRAD PHIHRHTDGR YYFTATAPEY DRIVLRRSRT LGGLSTAAES 100
    VIWRAHPTGD MAAHIWAPEL HRIGGKWYVY FAAAPAEDVW RIRIWVLENS 150
    HPDPFKGTWE EKGQVRTAWE TFSLDATTFT HRGARYLCWA QHEPGADNNT 200
    GLFLSEMANP WTLTGPQIRL STPEYDWECV GYKVNEGPYA LKRNGRIFLT 250
    YSASATDHHY CVGMFTADAG GNLMDPGNWS KSPIPVFTGN ETTKQYGPGH 300
    NCFTVAEDGR SDVLVYHARQ YKEIVGDP 328
    Length:328
    Mass (Da):36,774
    Last modified:October 1, 2000 - v1
    Checksum:iAA7D5C1D2ABF38D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023626 Genomic DNA. Translation: BAA90772.1.
    PIRiB59296.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023626 Genomic DNA. Translation: BAA90772.1 .
    PIRi B59296.

    3D structure databases

    ProteinModelPortali P82594.
    SMRi P82594. Positions 51-326.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH43. Glycoside Hydrolase Family 43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00667 .

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    InterProi IPR016828. Alpha-L-arabinofuranosidase.
    IPR006710. Glyco_hydro_43.
    IPR023296. Glyco_hydro_beta-prop.
    IPR006311. TAT_signal.
    [Graphical view ]
    PANTHERi PTHR22925. PTHR22925. 1 hit.
    Pfami PF04616. Glyco_hydro_43. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF025414. Alpha-L-arabinofuranosidase. 1 hit.
    SUPFAMi SSF75005. SSF75005. 1 hit.
    PROSITEi PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from Streptomyces chartreusis GS901."
      Matsuo N., Kaneko S., Kuno A., Kobayashi H., Kusakabe I.
      Biochem. J. 346:9-15(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-72, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Strain: GS901.

    Entry informationi

    Entry nameiIABF_STRCX
    AccessioniPrimary (citable) accession number: P82594
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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