Q12549 (XYN5_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase 5
Short name=Xylanase 5
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 5

Gene names

Name:

XYN5

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0. Ref.1 Temperature dependence: Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from direct assay. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 211	195	Endo-1,4-beta-xylanase 5		PRO_0000393172
Regions
	Compositional bias	86 – 92	7	Poly-Ser
Sites
	Active site	106	1	Nucleophile By similarity
	Active site	197	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12549 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B546955778BF1ED0	FASTA	211	22,794
	10 20 30 40 50 60 MKVTAAFASL LLTAFAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDEST GTFSMYWEDG 70 80 90 100 110 120 VSSDFVVGLG WTTGSSKSIT YSAQYSASSS SSYLAVYGWV NSPQAEYYIV EDYGDYNPCS 130 140 150 160 170 180 SATSLGTVYS DGSTYQVCTD TRRTRPSITG TSTFTQYFSV RESTRTSGTV TIANHFNFWA 190 200 210 QHGFGNSNFN YQVMAVEAWN GVGSASVTIS S

References

[1]

"Cloning of two beta-xylanase-encoding genes from Aspergillus niger and their expression in Saccharomyces cerevisiae." Luttig M., Pretorius I.S., van Zyl W.H. Biotechnol. Lett. 19:411-415(1997) Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 90196 / Alo MP-22.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39784 mRNA. Translation: AAA99065.1.
3D structure databases
HSSP	HSSP built from PDB template 1BK1 based on UniProtKB P33557.
ProteinModelPortal	Q12549.
SMR	Q12549. Positions 29-210.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
mycoCLAP	XYN11E_ASPNG.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	2.60.120.180. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Pfam	PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYN5_ASPNG

Accession

Primary (citable) accession number: Q12549

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	November 1, 1996
Last modified:	March 6, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program