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Q46684

- BGLX_DICCH

UniProt

Q46684 - BGLX_DICCH

Protein

Periplasmic beta-glucosidase/beta-xylosidase

Gene

bgxA

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Exhibits both beta-glucosidase and beta-xylosidase activities.

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
    Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei235 – 2351By similarity
    Active sitei360 – 3601By similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC
    2. xylan 1,4-beta-xylosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periplasmic beta-glucosidase/beta-xylosidase
    Including the following 2 domains:
    Beta-glucosidase (EC:3.2.1.21)
    Alternative name(s):
    Cellobiase
    Gentiobiase
    Beta-xylosidase (EC:3.2.1.37)
    Alternative name(s):
    1,4-beta-D-xylan xylohydrolase
    Xylan 1,4-beta-xylosidase
    Gene namesi
    Name:bgxA
    OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
    Taxonomic identifieri556 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 654629Periplasmic beta-glucosidase/beta-xylosidasePRO_0000011783Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ46684.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProiIPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.
    PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q46684-1 [UniParc]FASTAAdd to Basket

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    MEKSATRQKA LLIALPLLFS PLASAVQQAV LDTRGAPLIT VNGLTFKDLN    50
    RDGKLNPYED WRLPAAERAA DLVSRMTLAE KAGVMMHGSA PTAGSVTGAG 100
    TQYDLNAAKT MIADRYVNSF ITRLSGDNPA QMAEENNKLQ QLAEATRLGI 150
    PLTISTDPRS SFQSLVGVSV SVGKFSKWPE TLGLAAIGDE ELVRRFADIV 200
    RQEYRAVGIT EALSPQADLA TEPRWPRIDG TFGEDPDLTK KMVRGYVTGM 250
    QNGKNGLNAQ SVISIVKHWV GYGAAKDGWD SHNVYGKYAQ FRQNNLQWHI 300
    DPFTGAFEAH AAGIMPTYSI LRNASWHGKP IEQVGAGFNR FLLTDLLRGQ 350
    YGFDGVILSD WLITNDCKGD CLTGVKPGEK PVPRGMPWGV EKLTPAERFV 400
    KAVNAGVDQF GGVTDSALLV QAVQDGKLTE ARLDTSVNRI LKQKFQTGLF 450
    ERPYVNATQA NDIVGRADWQ QLADDTQARS LVLLQNNNLL PLRKGSRVWL 500
    HGIAANAAQE VGFIVVNTPE QADVALIRTH TPYEQPHKNF FFGSRHHEGS 550
    LAFRNDNPDY QAIVRASAKV PTLVTVYMER PAILTNVVDK TRAVVANFGV 600
    SDSVLLNRLM SGAAYTAKLP FELPSSMSAV RNQQPDLPYD SAKPLFPFGY 650
    GLPH 654
    Length:654
    Mass (Da):71,584
    Last modified:November 1, 1996 - v1
    Checksum:i5CEDFE62162A7A95
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08606 Genomic DNA. Translation: AAA80156.1.
    PIRiS53805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08606 Genomic DNA. Translation: AAA80156.1 .
    PIRi S53805.

    3D structure databases

    ProteinModelPortali Q46684.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProi IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.
    PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the bgxA gene from Erwinia chrysanthemi D1 which encodes a beta-glucosidase/xylosidase enzyme."
      Vroemen S., Heldens J., Boyd C., Henrissat B., Keen N.T.
      Mol. Gen. Genet. 246:465-477(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: D1.

    Entry informationi

    Entry nameiBGLX_DICCH
    AccessioniPrimary (citable) accession number: Q46684
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 69 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

    Multifunctional enzyme

    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