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Protein

Endo-1,4-beta-xylanase 1

Gene

xyl1

Organism
Claviceps purpurea (Ergot fungus) (Sphacelia segetum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

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 sitei112 – 1121NucleophilePROSITE-ProRule annotation
Active sitei203 – 2031Proton donorBy similarity

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

BRENDAi3.2.1.8. 1445.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_CLAPU.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 1 (EC:3.2.1.8)
Short name:
Xylanase 1
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 1
Gene namesi
Name:xyl1
OrganismiClaviceps purpurea (Ergot fungus) (Sphacelia segetum)
Taxonomic identifieri5111 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeClaviceps

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Leads to significant reduced xylanase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 216197Endo-1,4-beta-xylanase 1PRO_5000147292Add
BLAST

Expressioni

Inductioni

Expressed throughout the entire infection process during in infection of rye tissue.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO74716.
SMRiO74716. Positions 35-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 216188GH11PROSITE-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.
IPR018208. GH11_AS_1.
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.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O74716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTSVVSLV VGAISCVSAA PAAASELMQM TPRNSCYGGG LYSSYWADYG
60 70 80 90 100
NTRYSCGAGG HYDLSWGNGG NVVAGRGWKP ASPRAVTYSG SWQCNGNCYL
110 120 130 140 150
SVYGWTINPL VEYYIVENYG NYNPSAGAQR RGQVTADGSI YDIYISTQHN
160 170 180 190 200
QPSILGTNTF HQYWSIRRNK RVGGTVSTGV HFNAWRSLGM PLGTYDYMIV
210
ATEGFRSSGS ASITVS
Length:216
Mass (Da):23,339
Last modified:November 1, 1998 - v1
Checksum:i012E874E939E7581
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16969 Genomic DNA. Translation: CAA76570.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16969 Genomic DNA. Translation: CAA76570.1.

3D structure databases

ProteinModelPortaliO74716.
SMRiO74716. Positions 35-216.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_CLAPU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 1445.

Family and domain databases

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

Publicationsi

  1. "The xylanolytic system of Claviceps purpurea: cytological evidence for secretion of xylanases in infected rye tissue and molecular characterization of two xylanase genes."
    Giesbert S., Lepping H.B., Tenberge K.B., Tudzynski P.
    Phytopathology 88:1020-1030(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE.
    Strain: T5.

Entry informationi

Entry nameiXYN1_CLAPU
AccessioniPrimary (citable) accession number: O74716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 68 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.