Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable endo-1,4-beta-xylanase F3

Gene

xynF3

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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 sitei155Proton donorBy similarity1
Active sitei260NucleophileBy similarity1

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,4-beta-xylanase F3 (EC:3.2.1.8)
Short name:
Xylanase F3
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F3
Gene namesi
Name:xynF3
Synonyms:xlnF3
ORF Names:AFLA_008110
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_008110.

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_000039318720 – 324Probable endo-1,4-beta-xylanase F3Add BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi278 ↔ 284By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Expressed in presence of xylan and repressed by glucose.

Structurei

3D structure databases

ProteinModelPortaliB8NXJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 323GH10PROSITE-ProRule annotationAdd BLAST279

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000019847.
KOiK01181.
OMAiYLEVVNA.
OrthoDBiEOG092C45ID.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
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.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B8NXJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL
60 70 80 90 100
LQNSQNEAIV RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN
110 120 130 140 150
NKLVRGHTLV WHSQLPSWVQ GITDKDTLTE VIKNHITTIM QRYKGQIYAW
160 170 180 190 200
DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA FETAREADPN AKLYINDYNL
210 220 230 240 250
DSADYAKTKG MVSYVKKWLD AGVPIDGIVS LLPPRDEGLT SCTALTALAS
260 270 280 290 300
TGVSEVAVTE LDIEGASSES YLEVVNACLD VSSCVGITVW GVSDKDSWRS
310 320
STSPLLFDSN YQAKDAYNAI IDAL
Length:324
Mass (Da):35,239
Last modified:March 3, 2009 - v1
Checksum:iAD8AEFAF8EDB4496
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963486 Genomic DNA. Translation: EED44928.1.
RefSeqiXP_002385057.1. XM_002385016.1.

Genome annotation databases

EnsemblFungiiEED44928; EED44928; AFLA_008110.
GeneIDi7920217.
KEGGiafv:AFLA_008110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963486 Genomic DNA. Translation: EED44928.1.
RefSeqiXP_002385057.1. XM_002385016.1.

3D structure databases

ProteinModelPortaliB8NXJ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEED44928; EED44928; AFLA_008110.
GeneIDi7920217.
KEGGiafv:AFLA_008110.

Organism-specific databases

EuPathDBiFungiDB:AFLA_008110.

Phylogenomic databases

HOGENOMiHOG000019847.
KOiK01181.
OMAiYLEVVNA.
OrthoDBiEOG092C45ID.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
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.
PROSITEiPS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNF3_ASPFN
AccessioniPrimary (citable) accession number: B8NXJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 3, 2009
Last modified: November 2, 2016
This is version 40 of the entry and version 1 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

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.