Reviewed, UniProtKB/Swiss-Prot O69231 (XYNB_PAEBA)

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

Bacteria › Firmicutes › 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. 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	Direct protein sequencing
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro 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

Sequences

	Sequence		Length	Mass (Da)
	O69231-1 [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: 12698280] [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: 8998999] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ006646 Genomic DNA. Translation: CAA07174.1.
3D structure databases
HSSP	HSSP built from PDB template 1HIZ based on UniProtKB P40943.
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
Family and domain databases
InterPro	IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. False negative. [Graphical view]
ProtoNet	Search...

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:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)