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

Gene
N/A
Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Nucleophile
Active sitei177 – 1771Proton donor

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_TRIHA.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Endo-1,4-beta-xylanasePRO_0000184072Add
BLAST

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi14 – 196Combined sources
Beta strandi25 – 295Combined sources
Beta strandi34 – 418Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi59 – 8123Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 939Combined sources
Turni98 – 1014Combined sources
Beta strandi103 – 1108Combined sources
Beta strandi113 – 12513Combined sources
Beta strandi130 – 14314Combined sources
Beta strandi146 – 1516Combined sources
Helixi152 – 16110Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi182 – 1898Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNDX-ray2.00A1-190[»]
ProteinModelPortaliP48793.
SMRiP48793. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48793.

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.

P48793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QTIGPGTGYS NGYYYSYWND GHAGVTYTNG GGGSFTVNWS NSGNFVAGKG
60 70 80 90 100
WQPGTKNKVI NFSGSYNPNG NSYLSIYGWS RNPLIEYYIV ENFGTYNPST
110 120 130 140 150
GATKLGEVTS DGSVYDIYRT QRVNQPSIIG TATFYQYWSV RRNHRSSGSV
160 170 180 190
NTANHFNAWA SHGLTLGTMD YQIVAVEGYF SSGSASITVS
Length:190
Mass (Da):20,703
Last modified:February 1, 1996 - v1
Checksum:i6A0F4D1C3599C698
GO

Sequence databases

PIRiA44593.

Cross-referencesi

Sequence databases

PIRiA44593.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNDX-ray2.00A1-190[»]
ProteinModelPortaliP48793.
SMRiP48793. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_TRIHA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Miscellaneous databases

EvolutionaryTraceiP48793.

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. "The amino acid sequence of the 20 Kd xylanase from Trichoderma harzianum E58."
    Yaguchi M., Roy C., Watson D.C., Rollin F., Tan L.U.L., Senior D.J., Saddler J.N.
    (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.435-438, Elsevier, Amsterdam (1992)
    Cited for: PROTEIN SEQUENCE.
    Strain: E58.
  2. "High-resolution structures of xylanases from B.circulans and T.harzianum identify a new folding pattern and implications for the atomic basis of the catalysis."
    Campbell R.L., Rose D.R., Wakarchuk W.W., To R.J., Sung W., Yaguchi M.
    (In) Suominen P., Reinikainen T. (eds.); Trichoderma reesei cellulases and other hydrolases, pp.63-72, Foundation for Biotechnical and Industrial Fermentation Research, Helsinki (1993)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiXYN_TRIHA
AccessioniPrimary (citable) accession number: P48793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 74 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.