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P82593

- EABF_STRCX

UniProt

P82593 - EABF_STRCX

Protein

Extracellular exo-alpha-L-arabinofuranosidase

Gene
N/A
Organism
Streptomyces chartreusis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing polysaccharides and arabinoxylo-oligosaccharides. It leaves most of the polymer intact, including most of the main-chain residues and the arabinose side chains. It acts preferentially on the linear alpha-(1->2)-linked arabinofuranobiosides and alpha-(1->3)-linked arabinofuranobiosides, and is much less effective on alpha-(1->5)-linked arabinofuranobiosides. It also hydrolyzes the terminal alpha-(1->3)-linked arabinofuranotriosides in preference to the alpha-(1->5)-linked arabinofuranotriosides.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.5. The enzyme is slowly inactivated above pH 8.5 and below pH 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius. The enzyme is inactivated at temperatures above 45 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei58 – 581Alpha-L-arabinofuranoseBy similarity
    Binding sitei247 – 2471Alpha-L-arabinofuranose; via amide nitrogenBy similarity
    Active sitei380 – 3801Proton donor/acceptorBy similarity
    Sitei607 – 6071Important for substrate recognitionBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. L-arabinose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular exo-alpha-L-arabinofuranosidase (EC:3.2.1.55)
    Short name:
    ABF
    Alternative name(s):
    Alpha-L-AFase
    Extracellular arabinan exo-alpha-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 – 29291 PublicationAdd
    BLAST
    Chaini30 – 825796Extracellular exo-alpha-L-arabinofuranosidasePRO_0000012217Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP82593.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini70 – 215146CBM-cenCAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni379 – 3802Alpha-L-arabinofuranose bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR010720. Alpha-L-AF_C.
    IPR003305. CenC_carb-bd.
    IPR008985. ConA-like_lec_gl_sf.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF06964. Alpha-L-AF_C. 1 hit.
    PF02018. CBM_4_9. 1 hit.
    [Graphical view]
    SMARTiSM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P82593-1 [UniParc]FASTAAdd to Basket

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    MSRIRWRYGT AATALLVAAG LVPTATAHAE DVTDYSITVD PAAKGAAIDD    50
    TMYGVFFEDI NRAADGGLYA ELVQNRSFEY STDDNRSYTP LTSWIVDGTG 100
    EVVNDAGRLN ERNRNYLSLG AGSSVTNAGY NTGIRVEQGK RYDFSVWARA 150
    GSASTLTVAL KDAAGTLATA RQVAVEGGWA KYRATFTATR TSNRGRLAVA 200
    ANDAAALDMV SLFPRDTYRN QQNGLRKDLA EKIAALHPGF VRFPGGCLVN 250
    TGSMEDYSAA SGWQRKRSYQ WKDTVGPVEE RATNANFWGY NQSYGLGYYE 300
    YFRFSEDIGA MPLPVVPALV TGCGQNKAVD DEALLKRHIQ DTLDLIEFAN 350
    GPATSKWGKV RAEMGHPRPF RLTHLEVGNE ENLPDEFFDR FKQFRAAIEA 400
    EYPDITVVSN SGPDDAGTTF DTAWKLNREA NVEMVDEHYY NSPNWFLQNN 450
    DRYDSYDRGG PKVFLGEYAS QGNAWKNGLS EAAFMTGLER NADVVKLASY 500
    APLLANEDYV QWRPDLVWFN NRASWNSANY EVQKLFMNNV GDRVVPSKAT 550
    TTPDVSGPIT GAVGLSTWAT GTAYDDVKVT AADGATLLSD DFSGDASKWT 600
    HTGAGSWSVQ DGQYVQTDAA AENTMVQAGD PSWHDYDLHV KATKKSGKEG 650
    FLVAFGVKDT GNYYWWNLGG WNNTQSAVEQ AVDGGKGTLL TKAGSIETGR 700
    AYDIDVKVRG RQVTLYLDGQ EWGGFTDDKP AEPFRQVVTK DARTGDLIVK 750
    VVNAQPAEAR TAIDLGGARV ASTARVTTLA ADQDAVNTET DAPVTPATST 800
    FSGVTDRFTY TFPANSVTFL RLKQR 825
    Length:825
    Mass (Da):90,184
    Last modified:October 1, 2000 - v1
    Checksum:i9FF4EE99BE0C696E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023625 Genomic DNA. Translation: BAA90771.1.
    PIRiA59296.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023625 Genomic DNA. Translation: BAA90771.1 .
    PIRi A59296.

    3D structure databases

    ProteinModelPortali P82593.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    InterProi IPR010720. Alpha-L-AF_C.
    IPR003305. CenC_carb-bd.
    IPR008985. ConA-like_lec_gl_sf.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF06964. Alpha-L-AF_C. 1 hit.
    PF02018. CBM_4_9. 1 hit.
    [Graphical view ]
    SMARTi SM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF51445. SSF51445. 1 hit.
    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 30-75, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Strain: GS901.

    Entry informationi

    Entry nameiEABF_STRCX
    AccessioniPrimary (citable) accession number: P82593
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 61 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3