Q9LCB9 (3XYN2_VIBSX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-1,3-xylanase TXYA
EC=3.2.1.32

Alternative name(s):
Endo-1,3-beta-xylanase

Gene names

Name:

txyA

Organism

Vibrio sp.

Taxonomic identifier

678 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	460 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	Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Weakly active toward beta-1,3-xylotriose, yielding xylose and xylobiose. Converts beta-1,3-xylotetraose into xylotriose, xylobiose and xylose. Converts beta-1,3-xylopentaose into xylotetraose, xylotriose, xylobiose and xylose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, curdlan or carboxymethylcellulose. Ref.1 Ref.2
Catalytic activity	Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans. Ref.1 Ref.2
Enzyme regulation	Completely inhibited by Cu2+, Hg2+ and N-bromosuccinimide. Strongly inhibited by Ag+, Zn2+ and Pb2+. Moderately inhibited by Fe3+, Al3+, Mn2+, dithiothreitol and p-chloromercuribenzoic acid. Slightly activated by Mg2+ and Ca2+. Unaffected by Na+, K+, Ba2+, EDTA, iodoacetic acid and N-ethylmalaimide. Ref.2
Induction	By beta-1,3-xylan. Ref.2
Domain	The carbohydrate binding module (CBM) binds to insoluble beta-1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-1,4-mannan, curdlan, chitin, or soluble polysaccharides By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 26 family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0. Stable between pH 5.0 and 8.0. Ref.2 Temperature dependence: Optimum temperature is 37 degrees Celsius. Stable below 30 degrees Celsius. Ref.2

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 direct assay Ref.1. Source: UniProtKB
Molecular_function	polysaccharide binding Inferred from sequence or structural similarity. Source: UniProtKB xylan 1,3-beta-xylosidase activity Inferred from direct assay Ref.1. Source: UniProtKB xylan endo-1,3-beta-xylosidase 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
	Signal peptide	1 – 22	22	Ref.1 Ref.2
	Chain	23 – 460	438	Beta-1,3-xylanase TXYA Ref.1 Ref.2		PRO_0000403221
Regions
	Region	368 – 460	93	Carbohydrate binding module (CBM)
Amino acid modifications
	Disulfide bond	373 ↔ 459		By similarity UniProtKB Q8RS40
	Disulfide bond	404 ↔ 409		By similarity UniProtKB Q8RS40

Sequences

	Sequence		Length	Mass (Da)
	Q9LCB9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6EFA748496BA092A	FASTA	460	51,324
	10 20 30 40 50 60 MKKLAKMISV ATLGACAFQA HALDGKLVPD QGILVSVGQD VDSVNDYSSA MGTTPAGVTN 70 80 90 100 110 120 YVGIVNLDGL STDADAGAGR NNIVELANQY PTSALIVGVS MNGEVQNVAN GQYNANIDTL 130 140 150 160 170 180 IRTLGEFDRP VYLRWAYEVD GPWNGHNTED LKQSFRHVYQ RIRELGYADN ISMVWQVASY 190 200 210 220 230 240 CPTAPGQLGT WWPGDDVVDW VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY 250 260 270 280 290 300 QLADLTYSTD PAKGTNRQAK TDQQIWSEWF EPFFQFMVDN QDILKGFTYI NADWDSQWRW 310 320 330 340 350 360 AAPYNEGYWG DSRVQVIPYI KQKWQETLSD PKFIRHSDEL FAQLGYGNSD GGNGGDNGGD 370 380 390 400 410 420 NGGDNGGETP ENCTDDFNFN YVSDNEIEVY HVDKGWSAGW NYLCLDDYCL SGTKSNGAFS 430 440 450 460 RSFSAQLGQT YKMTFKVEDI TGQGQQIIDK TVTFTNQVCN

References

[1]	"Cloning, sequencing, and expression in Escherichia coli of the new gene encoding beta-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214." Araki T., Hashikawa S., Morishita T. Appl. Environ. Microbiol. 66:1741-1743(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-41 AND 300-313, FUNCTION, CATALYTIC ACTIVITY. Strain: XY-214.
[2]	"Purification and characterization of beta-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214." Araki T., Tani S., Maeda K., Hashikawa S., Nakagawa H., Morishita T. Biosci. Biotechnol. Biochem. 63:2017-2019(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-38, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION. Strain: XY-214.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB029043 Genomic DNA. Translation: BAA94698.1.
3D structure databases
ProteinModelPortal	Q9LCB9.
SMR	Q9LCB9. Positions 23-346, 370-460.
ModBase	Search...
Protein family/group databases
CAZy	CBM31. Carbohydrate-Binding Module Family 31. GH26. Glycoside Hydrolase Family 26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16528.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR021016. Beta-xylanase. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF11606. AlcCBM31. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3XYN2_VIBSX

Accession

Primary (citable) accession number: Q9LCB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program