P84195 (XYNA_GLOTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Endo-1,4-beta-xylanase Xyn10A EC=3.2.1.4 EC=3.2.1.8
Organism	Gloeophyllum trabeum (Brown rot fungus)
Taxonomic identifier	104355 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetes incertae sedis › Gloeophyllales › Gloeophyllaceae › Gloeophyllum

Protein attributes

Sequence length	45 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has xylanase, avicelase and cellobiohydrolase activity. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.1 Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.1
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted › extracellular space Ref.1.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation Xylan degradation
Cellular component	Secreted
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from direct assay Ref.1. Source: UniProtKB xylan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay Ref.1. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from direct assay Ref.1. Source: UniProtKB endo-1,4-beta-xylanase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›45	›45	Endo-1,4-beta-xylanase Xyn10A		PRO_0000184066
Experimental info
	Non-adjacent residues	10 – 11	2
	Non-adjacent residues	22 – 23	2
	Non-terminal residue	1	1
	Non-terminal residue	45	1

Sequences

	Sequence		Length	Mass (Da)
	P84195 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 8C14D9073D3D8A86	FASTA	45	4,771
	10 20 30 40 LYMGTATDNG ATAMLNLVES LKYSWVPSTF SGQGAATPYD SNLVK

References

[1]

"Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum." Cohen R., Suzuki M.R., Hammel K.E. Appl. Environ. Microbiol. 71:2412-2417(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Strain: ATCC 11539.

Cross-references

3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_GLOTR

Accession

Primary (citable) accession number: P84195

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	September 5, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program