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Protein

Probable endo-1,4-beta-xylanase B

Gene

xlnB

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 similarity

Catalytic activityi

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

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)DescriptionActionsGraphical viewLength
Active sitei117NucleophilePROSITE-ProRule annotation1
Active sitei208Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayi
UPA00114

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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
Gene namesi
Name:xlnB
Synonyms:xynB, xynG1
ORF Names:AFUB_078210
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039316620 – 221Probable endo-1,4-beta-xylanase BAdd BLAST202

Structurei

3D structure databases

ProteinModelPortaliB0Y8Q8
SMRiB0Y8Q8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 221GH11PROSITE-ProRule annotationAdd BLAST189

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000179135
OrthoDBiEOG092C4K17
PhylomeDBiB0Y8Q8

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 1 hit

Sequencei

Sequence statusi: Complete.

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

B0Y8Q8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSFSSLVLA ASTVAGVLAT PGSEQYVELA KRQLTSSQTG TNNGYYYSFW
60 70 80 90 100
TDGGGQVTYT NGNGGQYQVD WNNCGNFVAG KGWNPASEKA VTYSGSWQTS
110 120 130 140 150
GNGYLSVYGW TTSPLVEFYI VESYGSYDPS TGATHLGTVE SDGATYNLYK
160 170 180 190 200
TTRTNAPSIQ GTATFDQYWS VRTSHRQSGT VTTKNHFDAW RNAGLQLGNF
210 220
DYMIVATEGY QSSGSATITV S
Length:221
Mass (Da):23,810
Last modified:April 8, 2008 - v1
Checksum:i730177E76983C1E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499599 Genomic DNA Translation: EDP49789.1

Genome annotation databases

EnsemblFungiiEDP49789; EDP49789; AFUB_078210

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499599 Genomic DNA Translation: EDP49789.1

3D structure databases

ProteinModelPortaliB0Y8Q8
SMRiB0Y8Q8
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDP49789; EDP49789; AFUB_078210

Phylogenomic databases

HOGENOMiHOG000179135
OrthoDBiEOG092C4K17
PhylomeDBiB0Y8Q8

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYNB_ASPFC
AccessioniPrimary (citable) accession number: B0Y8Q8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: April 8, 2008
Last modified: June 20, 2018
This is version 47 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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Main funding by: National Institutes of Health

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