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Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Paenibacillus barcinonensis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in plant xylan biodegradation, probably via the hydrolysis of short xylooligosaccharides resulting from extracellular xylan hydrolysis, once they have been transported inside cells. Shows similar activity on xylans of different rate of arabinose or methylglucuronic substitution. Also displays high activity on aryl-xylosides. Is active on xylotetraose and xylotriose, but does not hydrolyze xylobiose, indicating that XynB is a xylanase and not a beta-xylosidase.2 Publications

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.2 Publications

Enzyme regulationi

Completely inhibited by Ag2+, Cu2+, Hg2+, Mn2+, Pb2+ and Sn2+. Strongly inhibited by Fe2+ and Zn2+. Co2+ and Ni2+ cause little inhibition while Ca2+ and Mg2+ do not affect enzyme activity, and Ba2+ produces a small stimulating effect. Irreversibly inactivated by SDS in vitro.1 Publication

pH dependencei

Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5 to 10. Is still active at pH 12.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Loses 100% activity after incubation for 15 minutes at 50 degrees Celsius.1 Publication

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei134Proton donorBy similarity1
Active sitei241NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene namesi
Name:xynB
OrganismiPaenibacillus barcinonensis
Taxonomic identifieri198119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003661962 – 332Endo-1,4-beta-xylanase BAdd BLAST331

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Turni13 – 15Combined sources3
Beta strandi17 – 22Combined sources6
Helixi24 – 37Combined sources14
Beta strandi39 – 45Combined sources7
Helixi49 – 52Combined sources4
Beta strandi54 – 57Combined sources4
Helixi62 – 72Combined sources11
Turni73 – 75Combined sources3
Beta strandi77 – 80Combined sources4
Beta strandi86 – 88Combined sources3
Helixi91 – 94Combined sources4
Beta strandi99 – 101Combined sources3
Helixi104 – 121Combined sources18
Turni122 – 125Combined sources4
Beta strandi127 – 133Combined sources7
Helixi148 – 152Combined sources5
Helixi157 – 168Combined sources12
Beta strandi172 – 180Combined sources9
Helixi184 – 199Combined sources16
Beta strandi206 – 209Combined sources4
Beta strandi212 – 214Combined sources3
Helixi220 – 231Combined sources12
Turni232 – 234Combined sources3
Beta strandi236 – 247Combined sources12
Helixi261 – 280Combined sources20
Turni281 – 284Combined sources4
Beta strandi285 – 294Combined sources10
Helixi299 – 301Combined sources3
Beta strandi302 – 305Combined sources4
Beta strandi313 – 315Combined sources3
Helixi323 – 328Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EMCX-ray2.10A2-332[»]
3EMQX-ray2.73A2-332[»]
3EMZX-ray2.08A2-332[»]
ProteinModelPortaliO69231.
SMRiO69231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO69231.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 331GH10PROSITE-ProRule annotationAdd BLAST330

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O69231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE
60 70 80 90 100
EVHPREHEYT FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG
110 120 130 140 150
TASREMMLSR LKQHIDTVVG RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL
160 170 180 190 200
RLLGEDYLVQ AFNMAHEADP NALLFYNDYN ETDPVKREKI YNLVRSLLDQ
210 220 230 240 250
GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT ELDLSVFRHE
260 270 280 290 300
DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL
310 320 330
DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD
Length:332
Mass (Da):38,561
Last modified:August 1, 1998 - v1
Checksum:iDDEF7BCF17C8A72E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006646 Genomic DNA. Translation: CAA07174.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006646 Genomic DNA. Translation: CAA07174.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EMCX-ray2.10A2-332[»]
3EMQX-ray2.73A2-332[»]
3EMZX-ray2.08A2-332[»]
ProteinModelPortaliO69231.
SMRiO69231.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Miscellaneous databases

EvolutionaryTraceiO69231.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNB_PAEBA
AccessioniPrimary (citable) accession number: O69231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 66 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.