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Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Aspergillus niger
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.By similarity

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)DescriptionActionsGraphical viewLength
Active sitei157Proton donorBy similarity1
Active sitei263NucleophilePROSITE-ProRule annotation1

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

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,4-beta-xylanase C (EC:3.2.1.8)
Short name:
Xylanase C
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene namesi
Name:xlnC
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039319020 – 327Probable endo-1,4-beta-xylanase CAdd BLAST308

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi281 ↔ 287By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiC5J411.

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00003040.

Structurei

3D structure databases

ProteinModelPortaliC5J411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 326GH10PROSITE-ProRule annotationAdd BLAST272

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IH86. Eukaryota.
COG3693. LUCA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEiPS00591. GH10_1. 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.

C5J411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQIKVAALA MLFASQVLSE PIDPRQASVS IDTKFKAHGK KYLGNIGDQY
60 70 80 90 100
TLTKNSKTPA IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ
110 120 130 140 150
SNNKLIRGHT LVWHSQLPSW VQSITDKNTL IEVMKNHITT VMQHYKGKIY
160 170 180 190 200
AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR IAFETARAAD PNAKLYINDY
210 220 230 240 250
NLDSASYSKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG GAGISGALNA
260 270 280 290 300
LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS
310 320
WRSSSTPLLF DSNYNPKPAY DAIANAL
Length:327
Mass (Da):35,476
Last modified:March 23, 2010 - v2
Checksum:i90B2F71FFCA70A65
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11 – 13MLF → KLI in ACR83565 (Ref. 1) Curated3
Sequence conflicti23D → E in ACR83565 (Ref. 1) Curated1
Sequence conflicti77W → R in ACR83565 (Ref. 1) Curated1
Sequence conflicti123S → A in ACR83565 (Ref. 1) Curated1
Sequence conflicti132E → G in ACR83565 (Ref. 1) Curated1
Sequence conflicti208S → P in ACR83565 (Ref. 1) Curated1
Sequence conflicti268G → D in ACR83565 (Ref. 1) Curated1
Sequence conflicti283N → D in ACR83565 (Ref. 1) Curated1
Sequence conflicti321 – 323DAI → FAV in ACR83565 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ986225 mRNA. Translation: ACR83565.1.
EU848304 mRNA. Translation: ACJ26381.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ986225 mRNA. Translation: ACR83565.1.
EU848304 mRNA. Translation: ACJ26381.1.

3D structure databases

ProteinModelPortaliC5J411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00003040.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Proteomic databases

PaxDbiC5J411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IH86. Eukaryota.
COG3693. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNC_ASPNG
AccessioniPrimary (citable) accession number: C5J411
Secondary accession number(s): C6F1T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: November 30, 2016
This is version 30 of the entry and version 2 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.