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Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551Proton donorBy similarity
Active sitei261 – 2611NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB
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:
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:xynf10a
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 325306Endo-1,4-beta-xylanase CPRO_0000393188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi279 ↔ 285By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00008146.

Structurei

3D structure databases

ProteinModelPortaliQ0H904.
SMRiQ0H904. Positions 27-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000019847.
InParanoidiQ0H904.
KOiK01181.
OrthoDBiEOG7GJ6PM.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q0H904-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL
60 70 80 90 100
LQKSQNEAIV RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN
110 120 130 140 150
GKKVRGHTLV WHSQLPSWVS AISDKNTLTS VLKNHITTVM TRYKGQIYAW
160 170 180 190 200
DVVNEIFNED GSLRDSVFSR VLGEDFVRIA FETARSVDPS AKLYINDYNL
210 220 230 240 250
DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS SVKGALTALA
260 270 280 290 300
SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR
310 320
SGSSPLLFDS NYQPKAAYNA IIAAL
Length:325
Mass (Da):35,221
Last modified:March 23, 2010 - v2
Checksum:iBB2D1688371B3F92
GO

Sequence cautioni

The sequence EAL89839.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141V → A in ABA40421. 1 PublicationCurated
Sequence conflicti40 – 401K → R in ABA40421. 1 PublicationCurated
Sequence conflicti214 – 2141Y → C in ABA40421. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ156555 mRNA. Translation: ABA40421.1.
EF375874 Genomic DNA. Translation: ABN48479.1.
AAHF01000005 Genomic DNA. Translation: EAL89839.1. Sequence problems.
RefSeqiXP_751877.1. XM_746784.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008146; CADAFUAP00008146; CADAFUAG00008146.
GeneIDi3509139.
KEGGiafm:AFUA_4G09480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ156555 mRNA. Translation: ABA40421.1.
EF375874 Genomic DNA. Translation: ABN48479.1.
AAHF01000005 Genomic DNA. Translation: EAL89839.1. Sequence problems.
RefSeqiXP_751877.1. XM_746784.1.

3D structure databases

ProteinModelPortaliQ0H904.
SMRiQ0H904. Positions 27-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00008146.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00008146; CADAFUAP00008146; CADAFUAG00008146.
GeneIDi3509139.
KEGGiafm:AFUA_4G09480.

Phylogenomic databases

HOGENOMiHOG000019847.
InParanoidiQ0H904.
KOiK01181.
OrthoDBiEOG7GJ6PM.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of recombinant xylan degrading enzymes from Aspergillus fumigatus isolate SL1."
    Dabrowski S., Ahring B.K.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SL1.
  2. "Cloning and characterization of xynf10a gene from Aspergillus fumigatus MKU1."
    Thiagarajan S., Jeya M., Gunasekaran P.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MKU1.
  3. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiXYNC_ASPFU
AccessioniPrimary (citable) accession number: Q0H904
Secondary accession number(s): A3FG82, Q4WPJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: January 7, 2015
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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

External Data

Dasty 3

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 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.