O69231 (XYNB_PAEBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase B
Short name=Xylanase B
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B

Gene names

Name:

xynB

Organism

Paenibacillus barcinonensis

Taxonomic identifier

198119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.1 Ref.2
Enzyme regulation	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. Ref.2
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Cytoplasm. Note: Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Cytoplasmic xylanase subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5 to 10. Is still active at pH 12. Ref.2 Temperature dependence: Optimum temperature is 50 degrees Celsius. Loses 100% activity after incubation for 15 minutes at 50 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 332

331

Endo-1,4-beta-xylanase B

PRO_0000366196

Sites

Active site

134

1

Proton donor By similarity

Active site

241

1

Nucleophile By similarity

Secondary structure

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332

Helix Strand Turn

Details...

Helix

10 – 12

3

Turn

13 – 15

3

Beta strand

17 – 22

6

Helix

24 – 37

14

Beta strand

39 – 45

7

Helix

49 – 52

4

Beta strand

54 – 57

4

Helix

62 – 72

11

Turn

73 – 75

3

Beta strand

77 – 80

4

Beta strand

86 – 88

3

Helix

91 – 94

4

Beta strand

99 – 101

3

Helix

104 – 121

18

Turn

122 – 125

4

Beta strand

127 – 133

7

Helix

148 – 152

5

Helix

157 – 168

12

Beta strand

172 – 180

9

Helix

184 – 199

16

Beta strand

206 – 209

4

Beta strand

212 – 214

3

Helix

220 – 231

12

Turn

232 – 234

3

Beta strand

236 – 247

12

Helix

261 – 280

20

Turn

281 – 284

4

Beta strand

285 – 294

10

Helix

299 – 301

3

Beta strand

302 – 305

4

Beta strand

313 – 315

3

Helix

323 – 328

6

Sequences

	Sequence		Length	Mass (Da)
	O69231 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: DDEF7BCF17C8A72E	FASTA	332	38,561
	10 20 30 40 50 60 MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE EVHPREHEYT 70 80 90 100 110 120 FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG TASREMMLSR LKQHIDTVVG 130 140 150 160 170 180 RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL RLLGEDYLVQ AFNMAHEADP NALLFYNDYN 190 200 210 220 230 240 ETDPVKREKI YNLVRSLLDQ GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT 250 260 270 280 290 300 ELDLSVFRHE DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL 310 320 330 DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ006646 Genomic DNA. Translation: CAA07174.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O69231.

SMR

O69231. Positions 2-330.

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00114.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O69231.

Entry information

Entry name

XYNB_PAEBA

Accession

Primary (citable) accession number: O69231

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program