Reviewed, UniProtKB/Swiss-Prot P83513 (XY11A_PSEXY)

Names and origin

Protein names

Recommended name:
    Bifunctional xylanase/deacetylase
Including the following 2 domains:
    1- Recommended name:
            Endo-1,4-beta-xylanase 11A
              EC=3.2.1.8
        Alternative name(s):
            Xylanase xyn11A
            Xylanase xynT
    2- Recommended name:
            Acetylated xylan deacetylase
              EC=3.5.1.-

Gene names

Name:	xyn11A
Synonyms:	xynT

Organism

Pseudobutyrivibrio xylanivorans

Taxonomic identifier

185007 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Pseudobutyrivibrio

Protein attributes

Sequence length	602 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	Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is also probably able, via its C-terminal domain, to remove acetyl groups from acetylated xylan, and thus it is probably capable of hydrolyzing acetylated xylan. Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.2
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted. Ref.2
Domain	Consists of three domains: two complementary catalytic domains and one substrate-binding module. Ref.1
Post-translational modification	In the later growth phases, seems to undergo a proteolytic cleavage into a 30 kDa protein possessing xylanolytic activity.
Biotechnological use	Could be used as a feed additive for animals in order to diminish health problems due to undigested plant fiber and enhance proliferation of beneficial microflora. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. Contains 1 CBM6 (carbohydrate binding type-6) domain. Contains 1 polysaccharide deacetylase domain.
biophysicochemical properties	pH dependence: Optimum pH is 5.6. Active from pH 4.0 to 8.0. Temperature dependence: Optimum temperature is 38 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	xylan catabolic process Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds 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 – 14	14	Ref.2
	Chain	15 – 602	588	Bifunctional xylanase/deacetylase		PRO_0000184070
Regions
	Domain	249 – 366	118	CBM6
	Domain	397 – 517	121	Polysaccharide deacetylase
	Region	24 – 210	187	Endoglucanase
Sites
	Active site	108	1	Nucleophile By similarity
	Active site	198	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83513-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: F3D7AE32EF7A3CF0	FASTA	602	65,923
	10 20 30 40 50 60 MSATLLVPSM TVKAADTIYN NKTGNQDGYD YELWKDTGNT SMTLNAGGTF DCSWSNINNA 70 80 90 100 110 120 LFRKGKKFDS TQTYQQIGNI TFDYGCDYRP NGNSYLCVYG WTVDPLVEYY IVDSWGTWRP 130 140 150 160 170 180 PGGTPKGQIQ VDGGTYDVYE TTRYNAPSIQ GDTTFKQYFS VRTSKRTSGT ISVSEHFKAW 190 200 210 220 230 240 ERMGMRCGNF MKPALNIEGY QSSGSASVYK NNMTIGGSSS SSGNQGGNQG GNTGNENAGN 250 260 270 280 290 300 NLVTVADADK IQCETMTKSG QYTGNISSPF NGVALYANND AVKYTQYFAS GTHDFTLRGC 310 320 330 340 350 360 SNNNKMARVD LKIGGQNKGT FYYGDSYPAE YTIKNVSHGT GNQTIELVVT ADDGQWDAYL 370 380 390 400 410 420 DYFNNSVEPG CSLVPGAVVV LVALGSSSNT GNNSGTNTQN QKLIALTFDD GPSSTTSQVL 430 440 450 460 470 480 DMLEKYNVKA TFFLIGQNVN SNTASIVQRQ VKMGCELACH SYTHEDMTKM NASQIRNQID 490 500 510 520 530 540 WTASAIKNTA GVDVKFFRPP YISVNNTMYQ NIDLPFIQGS MHNDWESSTS ASQRVNSVLS 550 560 570 580 590 600 SAKDGDIILL HDFQGNSQTV SALPQIIEGL KNQGYTFVTV SELFEMKGVN PNVEYKIWSN VK

References

[1]

"Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorcans Mz5T." Cepeljnik T., Rincon M.T., Flint H.J., Marinsek-Logar R. Folia Microbiol. (Praha) 51:263-267(2006) [PubMed: 17007421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN ORGANIZATION. Strain: Mz5T.

[2]

"Isolation and characterization of the Pseudobutyrivibrio xylanivorans Mz5T xylanase XynT -- the first family 11 endoxylanase from rumen Butyrivibrio-related bacteria." Cepeljnik T., Krizaj I., Marinsek-Logar R. Enzyme Microb. Technol. 34:219-227(2004) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-193, PROTEIN SEQUENCE OF 15-39, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, BIOTECHNOLOGY. Strain: Mz5T.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ543424 Genomic DNA. Translation: CAD65888.2.
3D structure databases
HSSP	HSSP built from PDB template 1F5J based on UniProtKB P77853.
ModBase	Search...
Protein family/group databases
CAZy	CBM36. Carbohydrate-Binding Module Family 36. GH11. Glycoside Hydrolase Family 11.
Enzyme and pathway databases
BRENDA	3.2.1.8. 276602.
Family and domain databases
InterPro	IPR005084. CBM_6. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. IPR002509. Polysac_deacetylase. [Graphical view]
Gene3D	G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit. G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.
Pfam	PF03422. CBM_6. 1 hit. PF00457. Glyco_hydro_11. 1 hit. PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
PROSITE	PS51175. CBM6. 1 hit. PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XY11A_PSEXY

Accession

Primary (citable) accession number: P83513

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	May 30, 2006
Last modified:	May 26, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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