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Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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.2 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is 4.9.1 Publication

Temperature dependencei

Optimum temperature is 52 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 sitei154Proton donorBy similarity1
Active sitei262NucleophileBy similarity1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.2.1.8 517
UniPathwayi
UPA00114

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10

Names & Taxonomyi

Protein namesi
Recommended name:
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
34 kDa xylanase
Xylanase X34
Gene namesi
Name:xlnC
ORF Names:AN1818
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VII
  • UP000005890 Componenti: Unassembled WGS sequence

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 – 24By similarityAdd BLAST24
ChainiPRO_000000797425 – 327Endo-1,4-beta-xylanase CAdd BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi280 ↔ 2861 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ00177

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.1 Publication

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ00177
SMRiQ00177
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00177

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 325GH10PROSITE-ProRule annotationAdd BLAST282

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000019847
InParanoidiQ00177
KOiK01181
OrthoDBiEOG092C45ID

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
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
PS51760 GH10_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q00177-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVHLKTLAGS AVFASLATAA VLPRQSASLN DLFVAAGKSY FGTCSDQALL
60 70 80 90 100
QNSQNEAIVA SQFGVITPEN SMKWDALEPS QGNFGWSGAD YLVDYATQHN
110 120 130 140 150
KKVRGHTLVW HSQLPSWVSS IGDANTLRSV MTNHINEVVG RYKGKIMHWD
160 170 180 190 200
VVNEIFNEDG TFRNSVFYNL LGEDFVRIAF ETARAADPDA KLYINDYNLD
210 220 230 240 250
SASYAKTQAM ASYVKKWLAE GVPIDGIGSQ AHYSSSHWSS TEAAGALSSL
260 270 280 290 300
ANTGVSEVAI TELDIAGAAS SDYLNLLNAC LNEQKCVGIT VWGVSDKDSW
310 320
RASDSPLLFD GNYQPKDAYN AIVNALS
Length:327
Mass (Da):35,441
Last modified:November 1, 1996 - v1
Checksum:iB59CF4DE435F6F20
GO

Sequence cautioni

The sequence CBF85620 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAA64983 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49894 Genomic DNA Translation: CAA90075.1
DQ490475 mRNA Translation: ABF50851.1
AACD01000029 Genomic DNA Translation: EAA64983.1 Sequence problems.
BN001307 Genomic DNA Translation: CBF85620.1 Sequence problems.
PIRiJC5034
RefSeqiXP_659422.1, XM_654330.1

Genome annotation databases

EnsemblFungiiEAA64983; EAA64983; AN1818.2
GeneIDi2874673
KEGGiani:AN1818.2

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49894 Genomic DNA Translation: CAA90075.1
DQ490475 mRNA Translation: ABF50851.1
AACD01000029 Genomic DNA Translation: EAA64983.1 Sequence problems.
BN001307 Genomic DNA Translation: CBF85620.1 Sequence problems.
PIRiJC5034
RefSeqiXP_659422.1, XM_654330.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TA3X-ray1.70B25-327[»]
ProteinModelPortaliQ00177
SMRiQ00177
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10 Glycoside Hydrolase Family 10

Proteomic databases

PRIDEiQ00177

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA64983; EAA64983; AN1818.2
GeneIDi2874673
KEGGiani:AN1818.2

Phylogenomic databases

HOGENOMiHOG000019847
InParanoidiQ00177
KOiK01181
OrthoDBiEOG092C45ID

Enzyme and pathway databases

UniPathwayi
UPA00114

BRENDAi3.2.1.8 517

Miscellaneous databases

EvolutionaryTraceiQ00177

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
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
PS51760 GH10_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXYNC_EMENI
AccessioniPrimary (citable) accession number: Q00177
Secondary accession number(s): C8VPM8, Q1HFU9, Q5BCB2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 20, 2018
This is version 119 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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