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Q46684

- BGLX_DICCH

UniProt

Q46684 - BGLX_DICCH

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MEKSATRQKA LLIALPLLFS PLASAVQQAV LDTRGAPLIT VNGLTFKDLN
60 70 80 90 100
RDGKLNPYED WRLPAAERAA DLVSRMTLAE KAGVMMHGSA PTAGSVTGAG
110 120 130 140 150
TQYDLNAAKT MIADRYVNSF ITRLSGDNPA QMAEENNKLQ QLAEATRLGI
160 170 180 190 200
PLTISTDPRS SFQSLVGVSV SVGKFSKWPE TLGLAAIGDE ELVRRFADIV
210 220 230 240 250
RQEYRAVGIT EALSPQADLA TEPRWPRIDG TFGEDPDLTK KMVRGYVTGM
260 270 280 290 300
QNGKNGLNAQ SVISIVKHWV GYGAAKDGWD SHNVYGKYAQ FRQNNLQWHI
310 320 330 340 350
DPFTGAFEAH AAGIMPTYSI LRNASWHGKP IEQVGAGFNR FLLTDLLRGQ
360 370 380 390 400
YGFDGVILSD WLITNDCKGD CLTGVKPGEK PVPRGMPWGV EKLTPAERFV
410 420 430 440 450
KAVNAGVDQF GGVTDSALLV QAVQDGKLTE ARLDTSVNRI LKQKFQTGLF
460 470 480 490 500
ERPYVNATQA NDIVGRADWQ QLADDTQARS LVLLQNNNLL PLRKGSRVWL
510 520 530 540 550
HGIAANAAQE VGFIVVNTPE QADVALIRTH TPYEQPHKNF FFGSRHHEGS
560 570 580 590 600
LAFRNDNPDY QAIVRASAKV PTLVTVYMER PAILTNVVDK TRAVVANFGV
610 620 630 640 650
SDSVLLNRLM SGAAYTAKLP FELPSSMSAV RNQQPDLPYD SAKPLFPFGY

GLPH
Length:654
Mass (Da):71,584
Last modified:November 1, 1996 - v1
Checksum:i5CEDFE62162A7A95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08606 Genomic DNA. Translation: AAA80156.1.
PIRiS53805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 70 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