Q9HFA4 (XYNA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase G2
Short name=Xylanase G2

Gene names

Name:	xlnA
Synonyms:	xlnG2, xynG2
ORF Names:	AO090120000026

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	232 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. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted Ref.4.
Miscellaneous	The promoter contains two 5'-GGCTAAA-3' sequences identified as binding sites for the xylanolytic transcriptional activator xlnR.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Biophysicochemical properties	Kinetic parameters: KM=242.8 µM for birch wood xylan Ref.1 Vmax=123 µmol/min/mg enzyme pH dependence: Optimum pH is 6.0. Retains over 95 percent activity in the pH range from 5.0 to 7.0, and 70 percent activity in the pH range from 4.0 to 8.0. Temperature dependence: Optimum temperature is 58 degrees Celsius. Has complete stability at 60 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from direct assay Ref.1. 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 Ref.1. 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 – 232	213	Endo-1,4-beta-xylanase A		PRO_0000393162
Sites
	Active site	128	1	Nucleophile By similarity
	Active site	219	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	34	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9HFA4 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1F73104751EA561C	FASTA	232	24,605
	10 20 30 40 50 60 MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST GYNNGYYYSF 70 80 90 100 110 120 WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR AITYSGSFNP SGNGYLAVYG 130 140 150 160 170 180 WTTDPLIEYY IVESYGTYNP GSGGTYKGQV TSDGGTYNIY TSVRTNAPSI IGTATFTQFW 190 200 210 220 230 SVRTSKRVGG TVTTGNHFNA WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, overexpression, and purification of a major xylanase from Aspergillus oryzae." Kimura T., Suzuki H., Furuhashi H., Aburatani T., Morimoto K., Karita S., Sakka K., Ohmiya K. Biosci. Biotechnol. Biochem. 64:2734-2738(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-64, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Gene cloning, sequencing, expression and characterization of a beta-xylanase gene from Aspergillus oryzae VTCC-F187." Quyen D.T., Nguyen S.L.T. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VTCC-F-187.
[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	EU848307 mRNA. Translation: ACJ26384.1. AB044941 Genomic DNA. Translation: BAB20794.1. AP007166 Genomic DNA. Translation: BAE62665.1.
PIR	JC7577.
RefSeq	XP_001823798.1. XM_001823746.2.
3D structure databases
HSSP	HSSP built from PDB template 1XYO based on UniProtKB P36217.
ProteinModelPortal	Q9HFA4.
SMR	Q9HFA4. Positions 46-231.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00010980.
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
mycoCLAP	XYN11A_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00011206; CADAORAP00010980; CADAORAG00011206.
GeneID	5996057.
KEGG	aor:AOR_1_38094.
Phylogenomic databases
eggNOG	NOG05353.
HOGENOM	HOG000179135.
OrthoDB	EOG4643MX.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16226.
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

XYNA_ASPOR

Accession

Primary (citable) accession number: Q9HFA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program