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Protein

Bifunctional xylanase/deacetylase

Gene

xyn11A

Organism
Pseudobutyrivibrio xylanivorans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.1 Publication

pH dependencei

Optimum pH is 5.6. Active from pH 4.0 to 8.0.

Temperature dependencei

Optimum temperature is 38 degrees Celsius.

Pathway:ixylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081NucleophilePROSITE-ProRule annotation
Active sitei198 – 1981Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17647.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11T_PSEXY.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional xylanase/deacetylase
Including the following 2 domains:
Endo-1,4-beta-xylanase 11A (EC:3.2.1.8)
Alternative name(s):
Xylanase XynT
Xylanase xyn11A
Acetylated xylan deacetylase (EC:3.5.1.-)
Gene namesi
Name:xyn11A
Synonyms:xynT
OrganismiPseudobutyrivibrio xylanivorans
Taxonomic identifieri185007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceaePseudobutyrivibrio

Subcellular locationi

  • Secreted Curated1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 14141 PublicationAdd
BLAST
Chaini15 – 602588Bifunctional xylanase/deacetylasePRO_0000184070Add
BLAST

Post-translational modificationi

In the later growth phases, seems to undergo a proteolytic cleavage into a 30 kDa protein possessing xylanolytic activity.

Structurei

3D structure databases

ProteinModelPortaliP83513.
SMRiP83513. Positions 18-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 366118CBM6PROSITE-ProRule annotationAdd
BLAST
Domaini402 – 578177NodB homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 210187EndoglucanaseAdd
BLAST

Domaini

Consists of three domains: two complementary catalytic domains and one substrate-binding module.1 Publication

Sequence similaritiesi

Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation
Contains 1 NodB homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
3.20.20.370. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83513-1 [UniParc]FASTAAdd to basket

« Hide

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

VK
Length:602
Mass (Da):65,923
Last modified:May 30, 2006 - v2
Checksum:iF3D7AE32EF7A3CF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ543424 Genomic DNA. Translation: CAD65888.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ543424 Genomic DNA. Translation: CAD65888.2.

3D structure databases

ProteinModelPortaliP83513.
SMRiP83513. Positions 18-363.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11T_PSEXY.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciMetaCyc:MONOMER-17647.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
3.20.20.370. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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.

Entry informationi

Entry nameiXY11A_PSEXY
AccessioniPrimary (citable) accession number: P83513
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: May 30, 2006
Last modified: April 29, 2015
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.