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P83513

- XY11A_PSEXY

UniProt

P83513 - XY11A_PSEXY

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Protein
Bifunctional xylanase/deacetylase
Gene
xyn11A, xynT
Organism
Pseudobutyrivibrio xylanivorans
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Nucleophile By similarity
Active sitei198 – 1981Proton donor By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
  3. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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.

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 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
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 Publication
Add
BLAST
Chaini15 – 602588Bifunctional xylanase/deacetylase
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 366118CBM6
Add
BLAST
Domaini402 – 578177NodB homology
Add
BLAST

Region

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

Domaini

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

Sequence similaritiesi

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.
IPR008985. ConA-like_lec_gl_sf.
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

MSATLLVPSM TVKAADTIYN NKTGNQDGYD YELWKDTGNT SMTLNAGGTF    50
DCSWSNINNA LFRKGKKFDS TQTYQQIGNI TFDYGCDYRP NGNSYLCVYG 100
WTVDPLVEYY IVDSWGTWRP PGGTPKGQIQ VDGGTYDVYE TTRYNAPSIQ 150
GDTTFKQYFS VRTSKRTSGT ISVSEHFKAW ERMGMRCGNF MKPALNIEGY 200
QSSGSASVYK NNMTIGGSSS SSGNQGGNQG GNTGNENAGN NLVTVADADK 250
IQCETMTKSG QYTGNISSPF NGVALYANND AVKYTQYFAS GTHDFTLRGC 300
SNNNKMARVD LKIGGQNKGT FYYGDSYPAE YTIKNVSHGT GNQTIELVVT 350
ADDGQWDAYL DYFNNSVEPG CSLVPGAVVV LVALGSSSNT GNNSGTNTQN 400
QKLIALTFDD GPSSTTSQVL DMLEKYNVKA TFFLIGQNVN SNTASIVQRQ 450
VKMGCELACH SYTHEDMTKM NASQIRNQID WTASAIKNTA GVDVKFFRPP 500
YISVNNTMYQ NIDLPFIQGS MHNDWESSTS ASQRVNSVLS SAKDGDIILL 550
HDFQGNSQTV SALPQIIEGL KNQGYTFVTV SELFEMKGVN PNVEYKIWSN 600
VK 602
Length:602
Mass (Da):65,923
Last modified:May 30, 2006 - v2
Checksum:iF3D7AE32EF7A3CF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ543424 Genomic DNA. Translation: CAD65888.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ543424 Genomic DNA. Translation: CAD65888.2 .

3D structure databases

ProteinModelPortali P83513.
SMRi P83513. Positions 18-363.
ModBasei Search...

Protein family/group databases

CAZyi CBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BioCyci MetaCyc:MONOMER-17647.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
3.20.20.370. 1 hit.
InterProi IPR005084. CMB_fam6.
IPR008985. ConA-like_lec_gl_sf.
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 ]
Pfami PF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEi PS51175. CBM6. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: March 19, 2014
This is version 65 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

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