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Protein

Endo-1,4-beta-xylanase G

Gene

xynG

Organism
Verticillium dahliae (Verticillium wilt)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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. The most favorable substrate is beechwood xylan.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei127NucleophilePROSITE-ProRule annotation1
Active sitei218Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayi
UPA00114

Protein family/group databases

CAZyiGH11 Glycoside Hydrolase Family 11
mycoCLAPiXYN11G_VERDA

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase G (EC:3.2.1.8)
Short name:
Xylanase G
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase G
Gene namesi
Name:xynG
OrganismiVerticillium dahliae (Verticillium wilt)
Taxonomic identifieri27337 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeGlomerellalesPlectosphaerellaceaeVerticillium

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000042961620 – 250Endo-1,4-beta-xylanase GAdd BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi31N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ0ZHI9
SMRiQ0ZHI9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 231GH11PROSITE-ProRule annotationAdd BLAST189

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q0ZHI9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSFKSLLLA ASAFTAVLGR PFDSFDGPDV NITDADELLV RRQVTANSEG
60 70 80 90 100
THNGYFYSWW SDGGGQVTYT MGAGSRYSVT WKDTGNFVGG KGWNPGTGRT
110 120 130 140 150
INYGGSFSPQ GNGYLAVYGW TRNPLIEYYV VESYGTYNPG SGGQLKGTVT
160 170 180 190 200
TDGGTYNVYV STRTNQPSID GTRTFQQYWS VRTSKRVGGA VTMQNHFNAW
210 220 230 240 250
AQFGMNLGAH YYQIVATEGY QSSGPSDIYV QTQCKSLCDR GRVTWRDVVC
Length:250
Mass (Da):27,410
Last modified:August 22, 2006 - v1
Checksum:iE9AEDE784AE4D995
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ449069 Genomic DNA Translation: ABE02800.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ449069 Genomic DNA Translation: ABE02800.1

3D structure databases

ProteinModelPortaliQ0ZHI9
SMRiQ0ZHI9
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11 Glycoside Hydrolase Family 11
mycoCLAPiXYN11G_VERDA

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYNG_VERDA
AccessioniPrimary (citable) accession number: Q0ZHI9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: August 22, 2006
Last modified: November 22, 2017
This is version 49 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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Main funding by: National Institutes of Health

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