P29417 (XYNA_PENCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:

XYLP

Organism

Penicillium chrysogenum (Penicillium notatum)

Taxonomic identifier

5076 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium › Penicillium chrysogenum complex

Protein attributes

Sequence length	353 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	Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subunit structure	Monomer.
Subcellular location	Secreted.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 353	330	Endo-1,4-beta-xylanase		PRO_0000007975
Sites
	Active site	161	1	Proton donor By similarity
	Active site	267	1	Nucleophile By similarity
Experimental info
	Sequence conflict	153	1	L → F AA sequence Ref.2
	Sequence conflict	180	1	E → S AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29417 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: BF445C5E72FE2F94	FASTA	353	38,193
	10 20 30 40 50 60 MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI ADQGTLNGNP 70 80 90 100 110 120 KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV EFAETNGKLI RGHTLVWHSQ 130 140 150 160 170 180 LPSWVSSITD KTTLTDVMKN HITTVMKQYK GKLYAWDVVN EIFEEDGTLR DSVFSRVLGE 190 200 210 220 230 240 DFVRIAFETA READPEAKLY INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL 250 260 270 280 290 300 GAGAGAAASG ALNALASAGT EEVAVTELDI AGATSTDYVD VVNACLDQPK CVGITVWGVA 310 320 330 340 350 DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL HSD

References

[1]	"Cloning and structural organization of a xylanase-encoding gene from penicillium chrysogenum." Haas H., Friedlin E., Stoeffler G., Redl B. Gene 126:237-242(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.
[2]	"Purification, characterization and partial amino acid sequences of a xylanase produced by Penicillium chrysogenum." Haas H., Herfurth E., Stoeffler G., Redl B. Biochim. Biophys. Acta 1117:279-286(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 61-107; 109-123; 140-146; 153-180; 199-212 AND 228-237, CHARACTERIZATION. Strain: ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M98458 Genomic DNA. Translation: AAA16427.1.
PIR	JN0575.
3D structure databases
ProteinModelPortal	P29417.
SMR	P29417. Positions 30-325.
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
mycoCLAP	XYN10P_PENCH.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_PENCH

Accession

Primary (citable) accession number: P29417

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program