Reviewed, UniProtKB/Swiss-Prot P26223 (XYNB_BUTFI)

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

Butyrivibrio fibrisolvens

Taxonomic identifier

831 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Butyrivibrio

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	B.fibrisolvens is located in the rumen of ruminant animals, where it contributes to the animal's digestion of plant material by hydrolyzing hemicellulose with its xylanases.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Endo-1,4-beta-xylanase B		PRO_0000184062
Regions
	Region	69 – 307	239	Catalytic Potential
Sites
	Active site	150	1	Proton donor By similarity
	Active site	255	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26223-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: D2CC7A638FA0F317	FASTA	635	73,185
	10 20 30 40 50 60 MNLKTAYEPY FKIGAAISRW NLHTPAHTKL LAEQFNSFTC ENDMKPMYYL DREANKKDPE 70 80 90 100 110 120 KYNLSPALTF ENAIPYLEFA KDNKIAMRGH TLVWHNQTPK WFFCERYNEN FPMADRETIL 130 140 150 160 170 180 ARLESYIHGV LDFVQTNYPG IIYAWDVVNE IVDEGAFRKS IWTETVGEDF FIKAFEFARK 190 200 210 220 230 240 YAAPEVSLFY NDYETAQPWK RDFILEKVLG PLIDKKLIDG MGMQSHLLMD HPDISEYRTA 250 260 270 280 290 300 LEMYGSTGLQ IHITELDMHN ADPSEESMHA LATRYQEFFQ TYLDAKKSGK ANITSVTFWN 310 320 330 340 350 360 LLDENSWLSG FRRETSYPLV FKGKCEAKEA YYAVLKAAVS DDSIDKWVPD YSEEDYKLQG 370 380 390 400 410 420 MPTPDIKRFR ENIWQENEYN YEASYGFIPN LFAYLHNDDV KRDCMLVIPG GGYCMCCSHE 430 440 450 460 470 480 GELAAMEFYN RGMNAFVLSY TTDITMSVPL HKQPLEDISR AVRFIRKNAS KYNIDGKKLV 490 500 510 520 530 540 IMGFSAGSHV CGSLAVHFDD VKDNNPEYAD ISGRPDGVIL SYPVITTGRY THADSVRTLL 550 560 570 580 590 600 GANPTDEELT YFSLEKQVKD NTPPCFIWQT EEDSVVPVEN SYLFANALRE KKIPFAHYVF 610 620 630 PRGFHGLTVA NDEFFSGWSG GEYSMEQTMR ARFAV

References

[1]	"Cloning, sequencing and expression of a gene encoding a 73 kDa xylanase enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c." Lin L.-L., Thomson J.A. Mol. Gen. Genet. 228:55-61(1991) [PubMed: 1909424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: H17C.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X61495 Genomic DNA. Translation: CAA43712.1.
PIR	S16567.
3D structure databases
HSSP	HSSP built from PDB template 1B31 based on UniProtKB P56588.
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
Enzyme and pathway databases
BRENDA	3.2.1.8. 1431.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_BUTFI

Accession

Primary (citable) accession number: P26223

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 49 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)