Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.2 Publications

Enzyme regulationi

N-bromosuccinimide completely inhibits the catalytic activity.1 Publication

pH dependencei

Optimum pH is 3.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Pathwayi: xylan 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 sitei101 – 1011NucleophileBy similarity
Active sitei194 – 1941Proton 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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_PENPU.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene namesi
Name:xynB
OrganismiTalaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
Taxonomic identifieri1266744 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 208192Endo-1,4-beta-xylanase BPRO_0000429662Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ96W72.
SMRiQ96W72. Positions 27-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 207191GH11PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96W72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTAAFAGL LATTLAAPAT ELVTRSINYV QNYNGNLGAF SYNEGAGTFS
60 70 80 90 100
MYWQQGVSND FVVGLGRSTG SSNPITYSAS YSASGGSYLA VYGWVNSPQA
110 120 130 140 150
EYHVVEAYGN YNPCSSGSAT NLGTVSSDGG TYQVCTDTRV NQPSITGTST
160 170 180 190 200
FTQFFSVRQG SRTSGTVTIA NHFNFWAKHG FGNSNFNYQV VAVEAWSGTG

TASVTVSA
Length:208
Mass (Da):21,869
Last modified:December 1, 2001 - v1
Checksum:i6DC554A2CA97C6D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 197TTLAAPA → RHSPPLS in CAA90390 (PubMed:9099888).Curated
Sequence conflicti103 – 1031H → Y in CAA90390 (PubMed:9099888).Curated
Sequence conflicti178 – 1792KH → ND in CAA90390 (PubMed:9099888).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50050 mRNA. Translation: CAA90390.1.
AF359553 Genomic DNA. Translation: AAK50762.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50050 mRNA. Translation: CAA90390.1.
AF359553 Genomic DNA. Translation: AAK50762.1.

3D structure databases

ProteinModelPortaliQ96W72.
SMRiQ96W72. Positions 27-207.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_PENPU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and expression of the cDNA of endoxylanase B from Penicillium purpurogenum."
    Diaz R., Sapag A., Peirano A., Steiner J., Eyzaguirre J.
    Gene 187:247-251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Differences in expression of two endoxylanase genes (xynA and xynB) from Penicillium purpurogenum."
    Chavez R., Schachter K., Navarro C., Peirano A., Aguirre C., Bull P., Eyzaguirre J.
    Gene 293:161-168(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, INDUCTION.
  3. "Penicillium purpurogenum produces several xylanases: purification and properties of two of the enzymes."
    Belancic A., Scarpa J., Peirano A., Diaz R., Steiner J., Eyzaguirre J.
    J. Biotechnol. 41:71-79(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Entry informationi

Entry nameiXYNB_TALPU
AccessioniPrimary (citable) accession number: Q96W72
Secondary accession number(s): Q12666
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: December 1, 2001
Last modified: April 13, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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 one 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.