O94163 (XYNF1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase F1
Short name=Xylanase F1
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F1

Gene names

Name:	xynF1
Synonyms:	xlnF1
ORF Names:	AO090103000423

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	327 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.3
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted Ref.3.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.0. Ref.3 Temperature dependence: Optimum temperature is 60 degrees Celsius.
Sequence caution	The sequence BAE65852.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from direct assay Ref.3. 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.3. 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 – 327	308	Endo-1,4-beta-xylanase F1		PRO_0000393191
Sites
	Active site	155	1	Proton donor By similarity
	Active site	263	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	281 ↔ 287		By similarity
Experimental info
	Sequence conflict	190	1	N → D in BAE65852. Ref.2
	Sequence conflict	209	1	K → Q in BAE65852. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O94163 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 38B2F6374BAD3D0A	FASTA	327	35,402
	10 20 30 40 50 60 MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL LQNSQNEAIV 70 80 90 100 110 120 RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN NKLVRGHTLV WHSQLPSWVQ 130 140 150 160 170 180 GITDKDTLTE VIKNHITTIM QRYKGQIYAW DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA 190 200 210 220 230 240 FETAREADPN AKLYINDYNL DSADYAKTKG MVSYVKKWLD AGVPIDGIGS QSHYSANGFP 250 260 270 280 290 300 VSGAKGALTA LASTGVSEVA VTELDIEGAS SESYLEVVNA CLDVSSCVGI TVWGVSDKDS 310 320 WRSSTSPLLF DSNYQAKDAY NAIIDAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Repression of the expression of genes encoding xylanolytic enzymes in Aspergillus oryzae by introduction of multiple copies of the xynF1 promoter." Kitamoto N., Yoshino S., Ito M., Kimura T., Ohmiya K., Tsukagoshi N. Appl. Microbiol. Biotechnol. 50:558-563(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KBN616.
[2]	"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.
[3]	"Purification and characterization of the overexpressed Aspergillus oryzae xylanase, XynF1." Kitamoto N., Yoshino S., Ohmiya K., Tsukagoshi N. Biosci. Biotechnol. Biochem. 63:1791-1794(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011212 Genomic DNA. Translation: BAA75475.1. AP007174 Genomic DNA. Translation: BAE65852.1. Sequence problems.
3D structure databases
HSSP	HSSP built from PDB template 1BG4 based on UniProtKB P56588.
ProteinModelPortal	O94163.
SMR	O94163. Positions 28-327.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00010097.
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
mycoCLAP	XYN10F_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG3693.
HOGENOM	HOG000019847.
OrthoDB	EOG415KPD.
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNF1_ASPOR

Accession

Primary (citable) accession number: O94163
Secondary accession number(s): Q2TY21

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program