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Protein

Probable endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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.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

  • endo-1,4-beta-xylanase activity Source: AspGD

GO - Biological processi

  • xylan catabolic process Source: AspGD

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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
Synonyms:xynA
ORF Names:An03g00940
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006706 Componenti: Chromosome 6R

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_500021972620 – 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

PaxDbiA2QFV7
PRIDEiA2QFV7

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00003040

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 36Combined sources6
Turni37 – 39Combined sources3
Beta strandi41 – 47Combined sources7
Helixi49 – 53Combined sources5
Beta strandi54 – 56Combined sources3
Helixi57 – 65Combined sources9
Beta strandi67 – 73Combined sources7
Helixi77 – 80Combined sources4
Helixi90 – 101Combined sources12
Beta strandi105 – 116Combined sources12
Helixi119 – 122Combined sources4
Helixi127 – 144Combined sources18
Turni145 – 147Combined sources3
Beta strandi150 – 157Combined sources8
Beta strandi163 – 165Combined sources3
Helixi169 – 174Combined sources6
Helixi177 – 189Combined sources13
Beta strandi193 – 200Combined sources8
Helixi208 – 222Combined sources15
Beta strandi229 – 232Combined sources4
Helixi240 – 243Combined sources4
Helixi244 – 251Combined sources8
Beta strandi257 – 266Combined sources10
Helixi271 – 282Combined sources12
Beta strandi287 – 293Combined sources7
Helixi297 – 299Combined sources3
Helixi303 – 305Combined sources3
Beta strandi308 – 310Combined sources3
Helixi318 – 325Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XUYX-ray2.00A/B27-327[»]
ProteinModelPortaliA2QFV7
SMRiA2QFV7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000019847
OrthoDBiEOG092C45ID

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.

A2QFV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQIKVAALA MLFASQVLSE PIEPRQASVS 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
NLDSASYPKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG GAGISGALNA
260 270 280 290 300
LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS
310 320
WRSSSTPLLF DSNYNPKPAY TAIANAL
Length:327
Mass (Da):35,486
Last modified:March 6, 2007 - v1
Checksum:iB0769C723DD3CA09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270045 Genomic DNA Translation: CAK38067.1

Genome annotation databases

EnsemblFungiiCAK38067; CAK38067; An03g00940

Similar proteinsi

Entry informationi

Entry nameiXYNC_ASPNC
AccessioniPrimary (citable) accession number: A2QFV7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 6, 2007
Last modified: May 23, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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