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O69231

- XYNB_PAEBA

UniProt

O69231 - XYNB_PAEBA

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Protein
Endo-1,4-beta-xylanase B
Gene
xynB
Organism
Paenibacillus barcinonensis
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei134 – 1341Proton donor By similarity
Active sitei241 – 2411Nucleophile By similarity

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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
Note: Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 332331Endo-1,4-beta-xylanase B
PRO_0000366196Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123
Turni13 – 153
Beta strandi17 – 226
Helixi24 – 3714
Beta strandi39 – 457
Helixi49 – 524
Beta strandi54 – 574
Helixi62 – 7211
Turni73 – 753
Beta strandi77 – 804
Beta strandi86 – 883
Helixi91 – 944
Beta strandi99 – 1013
Helixi104 – 12118
Turni122 – 1254
Beta strandi127 – 1337
Helixi148 – 1525
Helixi157 – 16812
Beta strandi172 – 1809
Helixi184 – 19916
Beta strandi206 – 2094
Beta strandi212 – 2143
Helixi220 – 23112
Turni232 – 2343
Beta strandi236 – 24712
Helixi261 – 28020
Turni281 – 2844
Beta strandi285 – 29410
Helixi299 – 3013
Beta strandi302 – 3054
Beta strandi313 – 3153
Helixi323 – 3286

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EMCX-ray2.10A2-332[»]
3EMQX-ray2.73A2-332[»]
3EMZX-ray2.08A2-332[»]
ProteinModelPortaliO69231.
SMRiO69231. Positions 2-330.

Miscellaneous databases

EvolutionaryTraceiO69231.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
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.

Sequencei

Sequence statusi: Complete.

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

O69231-1 [UniParc]FASTAAdd to Basket

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MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE    50
EVHPREHEYT FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG 100
TASREMMLSR LKQHIDTVVG RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL 150
RLLGEDYLVQ AFNMAHEADP NALLFYNDYN ETDPVKREKI YNLVRSLLDQ 200
GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT ELDLSVFRHE 250
DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL 300
DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD 332
Length:332
Mass (Da):38,561
Last modified:August 1, 1998 - v1
Checksum:iDDEF7BCF17C8A72E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006646 Genomic DNA. Translation: CAA07174.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006646 Genomic DNA. Translation: CAA07174.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EMC X-ray 2.10 A 2-332 [» ]
3EMQ X-ray 2.73 A 2-332 [» ]
3EMZ X-ray 2.08 A 2-332 [» ]
ProteinModelPortali O69231.
SMRi O69231. Positions 2-330.
ModBasei Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Miscellaneous databases

EvolutionaryTracei O69231.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: a new subclass of family 10 xylanases."
    Gallardo O., Diaz P., Pastor F.I.J.
    Appl. Microbiol. Biotechnol. 61:226-233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: DSM 15478 / CECT 7022 / BP-23.
  2. "Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides."
    Blanco A., Diaz P., Martinez J., Lopez O., Soler C., Pastor F.I.J.
    FEMS Microbiol. Lett. 137:285-290(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: DSM 15478 / CECT 7022 / BP-23.

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: June 11, 2014
This is version 55 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

External Data

Dasty 3

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