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Protein

Endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Schizophyllum commune (Split gill fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes xylans into xylobiose and xylose.

Catalytic activityi

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

pH dependencei

Active over a very broad pH range.

Pathway: 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 sitei87 – 871Nucleophile1 Publication
Active sitei184 – 1841Proton 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.
mycoCLAPiXYN11A_SCHCO.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:XYNA
OrganismiSchizophyllum commune (Split gill fungus)
Taxonomic identifieri5334 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Endo-1,4-beta-xylanase APRO_0000184071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 1601 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi578458.XP_003038466.1.

Structurei

3D structure databases

ProteinModelPortaliP35809.
SMRiP35809. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SGTPSSTGTD GGYYYSWWTD GAGDATYQNN GGGSYTLTWS GNNGNLVGGK
60 70 80 90 100
GWNPGAASRS ISYSGTYQPN GNSYLSVYGW TRSSLIEYYI VESYGSYDPS
110 120 130 140 150
SAASHKGSVT CNGATYDILS TWRYNAPSID GTQTFEQFWS VRNPKKAPGG
160 170 180 190
SISGTVDVQC HFDAWKGLGM NLGSEHNYQI VATEGYQSSG TATITVT
Length:197
Mass (Da):20,979
Last modified:June 1, 1994 - v1
Checksum:i42C8074E67C1FBE9
GO

Sequence databases

PIRiA44597.

Cross-referencesi

Sequence databases

PIRiA44597.

3D structure databases

ProteinModelPortaliP35809.
SMRiP35809. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi578458.XP_003038466.1.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_SCHCO.

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.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Yaguchi M., Roy C., Ujiie M., Watson D.C., Wakarchuk W.
    (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.149-154, Elsevier, Amsterdam (1992)
    Cited for: PROTEIN SEQUENCE.
    Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
  2. "Amino acid sequence and thermostability of xylanase A from Schizophyllum commune."
    Oku T., Roy C., Watson D.C., Wakarchuk W., Campbell R., Yaguchi M., Jurasek L., Paice M.G.
    FEBS Lett. 334:296-300(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
    Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.
  3. "Identification of a glutamate residue at the active site of xylanase A from Schizophyllum commune."
    Bray M.R., Clarke A.J.
    Eur. J. Biochem. 219:821-827(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVE SITE GLU-87.
    Strain: ATCC 38548 / Delmar / 13 / IHEM 5263.

Entry informationi

Entry nameiXYNA_SCHCO
AccessioniPrimary (citable) accession number: P35809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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

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 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.