A2Q7I0 (XYNB_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable endo-1,4-beta-xylanase B
Short name=Xylanase B
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Endo-1,4-beta-xylanase G1
Short name=Xylanase G1

Gene names

Name:	xlnB
Synonyms:	xynB, xynG1
ORF Names:	An01g00780

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.
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.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular region Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	endo-1,4-beta-xylanase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 225	207	Probable endo-1,4-beta-xylanase B		PRO_5000219293
Sites
	Active site	121	1	Nucleophile By similarity
	Active site	212	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2Q7I0 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: C4B8BB007AB2B8FD	FASTA	225	24,057
	10 20 30 40 50 60 MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY YSFWTDGGGD 70 80 90 100 110 120 VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT FTPSGNGYLS VYGWTTDPLI 130 140 150 160 170 180 EYYIVESYGD YNPGSGGTYK GTVTSDGSVY DIYTATRTNA ASIQGTATFT QYWSVRQNKR 190 200 210 220 VGGTVTTSNH FNAWAKLGMN LGTHNYQIVA TEGYQSSGSS SITVQ

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM269952 Genomic DNA. Translation: CAK43456.1.
RefSeq	XP_001388522.1. XM_001388485.2.
3D structure databases
ProteinModelPortal	A2Q7I0.
SMR	A2Q7I0. Positions 39-224.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00000077; CADANGAP00000070; CADANGAG00000077.
GeneID	4978152.
KEGG	ang:ANI_1_94014.
Phylogenomic databases
HOGENOM	HOG000179135.
KO	K01181.
OrthoDB	EOG4643MX.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_ASPNC

Accession

Primary (citable) accession number: A2Q7I0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program