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Q46684 (BGLX_DICCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periplasmic beta-glucosidase/beta-xylosidase

Including the following 2 domains:

  1. Beta-glucosidase
    EC=3.2.1.21
    Alternative name(s):
    Cellobiase
    Gentiobiase
  2. Beta-xylosidase
    EC=3.2.1.37
    Alternative name(s):
    1,4-beta-D-xylan xylohydrolase
    Xylan 1,4-beta-xylosidase
Gene names
Name:bgxA
OrganismDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Exhibits both beta-glucosidase and beta-xylosidase activities.

Catalytic activity

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.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

xylan 1,4-beta-xylosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 654629Periplasmic beta-glucosidase/beta-xylosidase
PRO_0000011783

Sites

Active site2351 By similarity
Active site3601 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46684 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5CEDFE62162A7A95

FASTA65471,584
        10         20         30         40         50         60 
MEKSATRQKA LLIALPLLFS PLASAVQQAV LDTRGAPLIT VNGLTFKDLN RDGKLNPYED 

        70         80         90        100        110        120 
WRLPAAERAA DLVSRMTLAE KAGVMMHGSA PTAGSVTGAG TQYDLNAAKT MIADRYVNSF 

       130        140        150        160        170        180 
ITRLSGDNPA QMAEENNKLQ QLAEATRLGI PLTISTDPRS SFQSLVGVSV SVGKFSKWPE 

       190        200        210        220        230        240 
TLGLAAIGDE ELVRRFADIV RQEYRAVGIT EALSPQADLA TEPRWPRIDG TFGEDPDLTK 

       250        260        270        280        290        300 
KMVRGYVTGM QNGKNGLNAQ SVISIVKHWV GYGAAKDGWD SHNVYGKYAQ FRQNNLQWHI 

       310        320        330        340        350        360 
DPFTGAFEAH AAGIMPTYSI LRNASWHGKP IEQVGAGFNR FLLTDLLRGQ YGFDGVILSD 

       370        380        390        400        410        420 
WLITNDCKGD CLTGVKPGEK PVPRGMPWGV EKLTPAERFV KAVNAGVDQF GGVTDSALLV 

       430        440        450        460        470        480 
QAVQDGKLTE ARLDTSVNRI LKQKFQTGLF ERPYVNATQA NDIVGRADWQ QLADDTQARS 

       490        500        510        520        530        540 
LVLLQNNNLL PLRKGSRVWL HGIAANAAQE VGFIVVNTPE QADVALIRTH TPYEQPHKNF 

       550        560        570        580        590        600 
FFGSRHHEGS LAFRNDNPDY QAIVRASAKV PTLVTVYMER PAILTNVVDK TRAVVANFGV 

       610        620        630        640        650 
SDSVLLNRLM SGAAYTAKLP FELPSSMSAV RNQQPDLPYD SAKPLFPFGY GLPH 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08606 Genomic DNA. Translation: AAA80156.1.
PIRS53805.

3D structure databases

ProteinModelPortalQ46684.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLX_DICCH
AccessionPrimary (citable) accession number: Q46684
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries