Reviewed, UniProtKB/Swiss-Prot P23030 (XYNB_PSEFL)

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

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	592 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	Xylanase B contributes to hydrolyze hemicellulose, the major component of plant cell-walls.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan metabolism; hemicellulose degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 1 CBM2 (carbohydrate binding type-2) domain. Contains 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Ref.1
	Chain	38 – 592	555	Endo-1,4-beta-xylanase B		PRO_0000007978
Regions
	Domain	38 – 136	99	CBM2
	Domain	163 – 289	127	CBM6
	Compositional bias	135 – 162	28	Ser-rich (linker)
	Compositional bias	300 – 320	21	Ser-rich (linker)
Sites
	Active site	431	1	Proton donor By similarity
	Active site	530	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	39 ↔ 133		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23030-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: E081F6308EA2B93A	FASTA	592	63,411
	10 20 30 40 50 60 MTISASDYRH PGNFLKRTTA LLCVGTALTA LAFNASAACT YTIDSEWSTG FTANITLKND 70 80 90 100 110 120 TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG 130 140 150 160 170 180 STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN 190 200 210 220 230 240 NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN 250 260 270 280 290 300 YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 310 320 330 340 350 360 VSSSSSVQSS SSSSSSSAAS AKKFIGNITT SGAVRSDFTR YWNQITPENE SKWGSVEGTR 370 380 390 400 410 420 NVYNWAPLDR IYAYARQNNI PVKAHTFVWG AQSPSWLNNL SGPEVAVEIE QWIRDYCARY 430 440 450 460 470 480 PDTAMIDVVN EAVPGHQPAG YAQRAFGNNW IQRVFQLARQ YCPNSILILN DYNNIRWQHN 490 500 510 520 530 540 EFIALAKAQG NYIDAVGLQA HELKGMTAAQ VKTAIDNIWN QVGKPIYISE YDIGDTNDQV 550 560 570 580 590 QLQNFQAHFP VFYNHPHVHG ITSGICGGQD LDRRLRFDPG QWHTAPGNDV VD

References

[1]

"Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes." Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J. Biochem. J. 272:369-376(1990) [PubMed: 2125205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46. Strain: Sp. Cellulosa.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54523 Genomic DNA. Translation: CAA38389.1.
3D structure databases
HSSP	HSSP built from PDB template 1EXG based on UniProtKB P07986.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. CBM35. Carbohydrate-Binding Module Family 35. GH10. Glycoside Hydrolase Family 10.
Enzyme and pathway databases
BRENDA	3.2.1.8. 329.
Family and domain databases
InterPro	IPR001919. CBD_bac. IPR012291. CBD_carb_bd. IPR018366. CBM2_CS. IPR005084. CBM_6. IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00553. CBM_2. 1 hit. PF03422. CBM_6. 1 hit. PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00637. CBD_II. 1 hit. SM00633. Glyco_10. 1 hit. [Graphical view]
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS51175. CBM6. 1 hit. PS00591. GLYCOSYL_HYDROL_F10. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_PSEFL

Accession

Primary (citable) accession number: P23030

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 72 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)