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Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Aspergillus niger
Status
Reviewed-Annotation score: -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

Keywordsi

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

Enzyme and pathway databases

UniPathwayi
UPA00114

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10
mycoCLAPiXYN10B_ASPNG

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

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_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

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Structurei

3D structure databases

ProteinModelPortaliC5J411
SMRiC5J411
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IH86 Eukaryota
COG3693 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR031158 GH10_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00591 GH10_1, 1 hit
PS51760 GH10_2, 1 hit

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

Similar proteinsi

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
SMRiC5J411
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10
mycoCLAPiXYN10B_ASPNG

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IH86 Eukaryota
COG3693 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR031158 GH10_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00591 GH10_1, 1 hit
PS51760 GH10_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYNC_ASPNG
AccessioniPrimary (citable) accession number: C5J411
Secondary accession number(s): C6F1T1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: November 7, 2018
This is version 36 of the entry and version 2 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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