Q0H904 (XYNC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	xlnC
Synonyms:	xynf10a

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Induction	Expressed in presence of xylan and repressed by glucose.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Sequence caution	The sequence EAL89839.1 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 Reference 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 – 325	306	Endo-1,4-beta-xylanase C		PRO_0000393188
Sites
	Active site	155	1	Proton donor By similarity
	Active site	261	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	279 ↔ 285		By similarity
Experimental info
	Sequence conflict	14	1	V → A in ABA40421. Ref.1
	Sequence conflict	40	1	K → R in ABA40421. Ref.1
	Sequence conflict	214	1	Y → C in ABA40421. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q0H904 [UniParc]. Last modified March 23, 2010. Version 2. Checksum: BB2D1688371B3F92	FASTA	325	35,221
	10 20 30 40 50 60 MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV 70 80 90 100 110 120 RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS 130 140 150 160 170 180 AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA 190 200 210 220 230 240 FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGAGASS 250 260 270 280 290 300 SVKGALTALA SSGVSEVAIT ELDIAGASSQ DYVNVVKACL DVPKCVGITV WGVSDRDSWR 310 320 SGSSPLLFDS NYQPKAAYNA IIAAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of recombinant xylan degrading enzymes from Aspergillus fumigatus isolate SL1." Dabrowski S., Ahring B.K. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: SL1.
[2]	"Cloning and characterization of xynf10a gene from Aspergillus fumigatus MKU1." Thiagarajan S., Jeya M., Gunasekaran P. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MKU1.
[3]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ156555 mRNA. Translation: ABA40421.1. EF375874 Genomic DNA. Translation: ABN48479.1. AAHF01000005 Genomic DNA. Translation: EAL89839.1. Sequence problems.
RefSeq	XP_751877.1. XM_746784.1.
3D structure databases
ProteinModelPortal	Q0H904.
SMR	Q0H904. Positions 27-325.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00008146.
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3509139.
KEGG	afm:AFUA_4G09480.
Phylogenomic databases
HOGENOM	HOG000019847.
KO	K01181.
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

XYNC_ASPFU

Accession

Primary (citable) accession number: Q0H904
Secondary accession number(s): A3FG82, Q4WPJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	March 23, 2010
Last modified:	May 1, 2013
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program