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Protein

Endo-1,4-beta-xylanase 1

Gene

xyn1

Organism
Hypocrea jecorina (Trichoderma reesei)
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 sitei126 – 1261NucleophilePROSITE-ProRule annotation
Active sitei215 – 2151Proton 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

BRENDAi3.2.1.8. 6451.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_TRIRE.

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:xyn1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5151Sequence AnalysisAdd
BLAST
Chaini52 – 229178Endo-1,4-beta-xylanase 1PRO_0000008013Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI74223.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 616Combined sources
Beta strandi63 – 708Combined sources
Beta strandi72 – 8312Combined sources
Beta strandi85 – 939Combined sources
Beta strandi99 – 12123Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 13511Combined sources
Beta strandi140 – 1489Combined sources
Beta strandi151 – 16515Combined sources
Beta strandi168 – 18114Combined sources
Beta strandi184 – 1885Combined sources
Helixi190 – 19910Combined sources
Beta strandi206 – 22823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XYNX-ray2.00A52-229[»]
ProteinModelPortaliP36218.
SMRiP36218. Positions 52-229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36218.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.
OMAiNQYISVR.

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.

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

P36218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAFSSLICA LTSIASTLAM PTGLEPESSV NVTERGMYDF VLGAHNDHRR
60 70 80 90 100
RASINYDQNY QTGGQVSYSP SNTGFSVNWN TQDDFVVGVG WTTGSSAPIN
110 120 130 140 150
FGGSFSVNSG TGLLSVYGWS TNPLVEYYIM EDNHNYPAQG TVKGTVTSDG
160 170 180 190 200
ATYTIWENTR VNEPSIQGTA TFNQYISVRN SPRTSGTVTV QNHFNAWASL
210 220
GLHLGQMNYQ VVAVEGWGGS GSASQSVSN
Length:229
Mass (Da):24,583
Last modified:June 1, 1994 - v1
Checksum:iF9E8BFE1607038DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69574 Genomic DNA. Translation: CAA49294.1.
PIRiS39155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69574 Genomic DNA. Translation: CAA49294.1.
PIRiS39155.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XYNX-ray2.00A52-229[»]
ProteinModelPortaliP36218.
SMRiP36218. Positions 52-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI74223.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG05353.
OMAiNQYISVR.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6451.

Miscellaneous databases

EvolutionaryTraceiP36218.

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 two major xylanases from Trichoderma reesei: characterization of both enzymes and genes."
    Toerroenen A., Mach R.L., Messner R., Gonzalez R., Kalkkinen N., Harkki A., Kubicek C.P.
    Biotechnology (N.Y.) 10:1461-1465(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 56765 / Rut C-30.
  2. "Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei."
    Toerroenen A., Rouvinen J.
    Biochemistry 34:847-856(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiXYN1_HYPJE
AccessioniPrimary (citable) accession number: P36218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 1, 2015
This is version 91 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.