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

xlnB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 5 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.By similarity2 Publications

Catalytic activityi

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

Enzyme regulationi

Metal ions, copper, iron and N-bromosuccinimide decrease enzyme activity. Manganese, calcium, L-tryptophan, beta-mercaptoethanol, L-cysteine and dithiodipyridine stimulate the enzyme activity.1 Publication

pH dependencei

Optimum pH is 5.0. Retains about 76 percent of its activity after being incubated at pH 2.0 for 30 min at 37 degrees Celsius.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Displays about 95 percent of peak activity in the temperature range from 37 to 41 degrees Celsius.2 Publications

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 sitei121 – 1211NucleophilePROSITE-ProRule annotation
Active sitei212 – 2121Proton 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.

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
Endo-1,4-beta-xylanase G1
Short name:
Xylanase G1
Endo-1,4-beta-xylanase II
Short name:
Xylanase II
Gene namesi
Name:xlnB
Synonyms:xyn2, xynB, xynG1
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 3719PRO_0000007993Add
BLAST
Chaini38 – 225188Endo-1,4-beta-xylanase BPRO_0000007994Add
BLAST

Proteomic databases

PaxDbiP55330.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00000070.

Structurei

3D structure databases

ProteinModelPortaliP55330.
SMRiP55330. Positions 39-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 225189GH11PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHTC. Eukaryota.
ENOG410YH6C. LUCA.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
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.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. 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.

P55330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY
60 70 80 90 100
YSFWTDGGGD VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT
110 120 130 140 150
FTPSGNGYLS VYGWTTDPLI EYYIVESYGD YNPGSGGTYK GTVTSDGSVY
160 170 180 190 200
DIYTATRTNA ASIQGTATFT QYWSVRQNKR VGGTVTTSNH FNAWAKLGMN
210 220
LGTHNYQIVA TEGYQSSGSS SITVQ
Length:225
Mass (Da):24,057
Last modified:October 1, 1996 - v1
Checksum:iC4B8BB007AB2B8FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → V in AAM08362 (Ref. 2) Curated
Sequence conflicti16 – 161A → V in AAM95167 (Ref. 3) Curated
Sequence conflicti16 – 161A → V in ABA00146 (Ref. 4) Curated
Sequence conflicti16 – 161A → V in AAS46914 (Ref. 5) Curated
Sequence conflicti16 – 161A → V in ACA51680 (Ref. 7) Curated
Sequence conflicti25 – 262AQ → VE in AAM08362 (Ref. 2) Curated
Sequence conflicti25 – 262AQ → VE in AAM95167 (Ref. 3) Curated
Sequence conflicti25 – 262AQ → VE in ABA00146 (Ref. 4) Curated
Sequence conflicti25 – 262AQ → VE in AAS46914 (Ref. 5) Curated
Sequence conflicti25 – 262AQ → VE in ACA51680 (Ref. 7) Curated
Sequence conflicti33 – 331M → K in AAM08362 (Ref. 2) Curated
Sequence conflicti33 – 331M → K in AAM95167 (Ref. 3) Curated
Sequence conflicti33 – 331M → K in ABA00146 (Ref. 4) Curated
Sequence conflicti33 – 331M → K in AAS46914 (Ref. 5) Curated
Sequence conflicti33 – 331M → K in ACA51680 (Ref. 7) Curated
Sequence conflicti70 – 701A → S in AAM08362 (Ref. 2) Curated
Sequence conflicti70 – 701A → S in AAM95167 (Ref. 3) Curated
Sequence conflicti70 – 701A → S in ABA00146 (Ref. 4) Curated
Sequence conflicti70 – 701A → S in AAS46914 (Ref. 5) Curated
Sequence conflicti70 – 701A → S in ACA51680 (Ref. 7) Curated
Sequence conflicti76 – 761S → P in ACJ26382 (Ref. 8) Curated
Sequence conflicti130 – 1301D → V in ACA24724 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38071 Genomic DNA. Translation: BAA07265.1.
AF490982 mRNA. Translation: AAM08362.1.
AY126481 Genomic DNA. Translation: AAM95167.1.
DQ174549 Genomic DNA. Translation: ABA00146.1.
AY536639 mRNA. Translation: AAS46914.1.
EU423881 Genomic DNA. Translation: ACA24724.1.
EU430370 mRNA. Translation: ACA51680.1.
EU848305 mRNA. Translation: ACJ26382.1.
FJ772090 mRNA. Translation: ACN89393.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38071 Genomic DNA. Translation: BAA07265.1.
AF490982 mRNA. Translation: AAM08362.1.
AY126481 Genomic DNA. Translation: AAM95167.1.
DQ174549 Genomic DNA. Translation: ABA00146.1.
AY536639 mRNA. Translation: AAS46914.1.
EU423881 Genomic DNA. Translation: ACA24724.1.
EU430370 mRNA. Translation: ACA51680.1.
EU848305 mRNA. Translation: ACJ26382.1.
FJ772090 mRNA. Translation: ACN89393.1.

3D structure databases

ProteinModelPortaliP55330.
SMRiP55330. Positions 39-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00000070.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Proteomic databases

PaxDbiP55330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IHTC. Eukaryota.
ENOG410YH6C. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
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.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNB_ASPNG
AccessioniPrimary (citable) accession number: P55330
Secondary accession number(s): B1A5N7
, C0LVA6, C6F1T2, Q12557, Q8TG22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 13, 2016
This is version 85 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.