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Protein

Endo-1,4-beta-xylanase 1

Gene

xyn1

Organism
Humicola grisea var. thermoidea
Status
Reviewed-Annotation score: Annotation score: 3 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.

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 sitei150 – 1501Proton donorBy similarity
Active sitei257 – 2571NucleophileBy 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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH10. Glycoside Hydrolase Family 10.

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
OrganismiHumicola grisea var. thermoidea
Taxonomic identifieri5528 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 429410Endo-1,4-beta-xylanase 1PRO_0000429617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi286 ↔ 292By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Induced by xylan and Avicel, and repressed by glucose.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP79046.
SMRiP79046. Positions 395-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 336294GH10PROSITE-ProRule annotationAdd
BLAST
Domaini393 – 42937CBM1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi338 – 3414Poly-Ala
Compositional biasi356 – 38732Thr-richAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P79046-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTKSILTAA LLAAAPASAQ LHELAVKAGL KYFGTALREG AINSDQQYNR
60 70 80 90 100
ILSDTREFGQ LVPENGQKWD ATEPNRGQFN FQQGDITANK ARQNGQGLRC
110 120 130 140 150
HTLIWYSQLP GWVSSGNWNR QTLEAVMKTH IDNVMGHYKG QCYAWDVVNE
160 170 180 190 200
AVDDNGQWRN NVFLRVFGTD YLPLSFNLAK AADPDTKLYY NDYNLEYNQA
210 220 230 240 250
KTDRAVELVK IVQDAGAPID GVGFQGHLIV GSTPTRQQLA TVLRRFTSLG
260 270 280 290 300
VEVAYTELDI RHSRLPASQQ ALVTQGNDFA NVVGSCLDVA GCVGVTVWSF
310 320 330 340 350
TDKYSWIPET FSGEGDALIY DRNFNKKPAW TSISSVLAAA ATNPPASSST
360 370 380 390 400
SVVVPTTTFV TTTTTPPPIS SPIVPSTTTT SAVPTTTVSP PEPEQTRWGQ
410 420
CGGIGWNGPT KCQSPWTCTR LNDWYFQCL
Length:429
Mass (Da):47,018
Last modified:May 1, 1997 - v1
Checksum:i9B7A6B47A25FDE57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001030 Genomic DNA. Translation: BAA19220.1.
PIRiJC5861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001030 Genomic DNA. Translation: BAA19220.1.
PIRiJC5861.

3D structure databases

ProteinModelPortaliP79046.
SMRiP79046. Positions 395-429.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001000. GH10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYN1_HUMGT
AccessioniPrimary (citable) accession number: P79046
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: May 1, 1997
Last modified: March 16, 2016
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

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.