P87037 (XYNB_ASPOR) 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, xynG, xynG1
ORF Names:	AO090001000111

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	221 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.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted Ref.4.
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 – 19	19	Potential
	Chain	20 – 221	202	Probable endo-1,4-beta-xylanase B		PRO_0000393169
Sites
	Active site	117	1	Nucleophile By similarity
	Active site	208	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P87037 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: C010E11E5F53C77E	FASTA	221	23,746
	10 20 30 40 50 60 MVSFSSLLLA VSAVSGALAA PGDSTLVELA KRAITSSETG TNNGYYYSFW TNGGGDVEYT 70 80 90 100 110 120 NGNGGQYSVK WTNCDNFVAG KGWNPGSAKT VTYSGEWESN SNSYVSLYGW TQNPLVEYYI 130 140 150 160 170 180 VDKYGDYDPS TGATELGTVE SDGGTYKIYK TTRENAPSIE GTSTFNQYWS VRQSGRVGGT 190 200 210 220 ITAQNHFDAW ANVGLQLGTH NYMILATEGY KSSGSATITV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence of xylanase G1 gene from Aspergillus oryzae KBN616." Kimura T., Kitamoto N., Kito Y., Karita S., Sakka K., Ohmiya K. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: KBN616.
[2]	"Cloning and sequence analysis of the gene encoding xylanase from Aspergillus oryzae." Han W., Su Y., Chen G. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AS 3.4382.
[3]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.
[4]	"Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions." Oda K., Kakizono D., Yamada O., Iefuji H., Akita O., Iwashita K. Appl. Environ. Microbiol. 72:3448-3457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU586113 mRNA. Translation: ACB97629.1. AB003085 Genomic DNA. Translation: BAA19744.1. AP007154 Genomic DNA. Translation: BAE56664.1.
RefSeq	XP_001818666.1. XM_001818614.2.
3D structure databases
HSSP	HSSP built from PDB template 1HIX based on UniProtKB Q59962.
ProteinModelPortal	P87037.
SMR	P87037. Positions 32-220.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00000098.
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
mycoCLAP	XYN11G_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00000099; CADAORAP00000098; CADAORAG00000099.
GeneID	5990637.
KEGG	aor:AOR_1_174164.
Phylogenomic databases
eggNOG	NOG05353.
HOGENOM	HOG000179135.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_ASPOR

Accession

Primary (citable) accession number: P87037

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program