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P35809

- XYNA_SCHCO

UniProt

P35809 - XYNA_SCHCO

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Protein

Endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Schizophyllum commune (Split gill fungus)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Nucleophile1 Publication
Active sitei184 – 1841Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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

  1. extracellular region Source: UniProtKB-KW
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

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

PIRi A44597.

3D structure databases

ProteinModelPortali P35809.
SMRi P35809. Positions 3-196.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.
mycoCLAPi XYN11A_SCHCO.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 77 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