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P29417

- XYNA_PENCH

UniProt

P29417 - XYNA_PENCH

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Protein

Endo-1,4-beta-xylanase

Gene

XYLP

Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611Proton donorBy similarity
Active sitei267 – 2671NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.
mycoCLAPiXYN10P_PENCH.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Gene namesi
Name:XYLP
OrganismiPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifieri5076 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 353330Endo-1,4-beta-xylanasePRO_0000007975Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP29417.
SMRiP29417. Positions 30-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29417-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI
60 70 80 90 100
ADQGTLNGNP KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV
110 120 130 140 150
EFAETNGKLI RGHTLVWHSQ LPSWVSSITD KTTLTDVMKN HITTVMKQYK
160 170 180 190 200
GKLYAWDVVN EIFEEDGTLR DSVFSRVLGE DFVRIAFETA READPEAKLY
210 220 230 240 250
INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL GAGAGAAASG
260 270 280 290 300
ALNALASAGT EEVAVTELDI AGATSTDYVD VVNACLDQPK CVGITVWGVA
310 320 330 340 350
DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL

HSD
Length:353
Mass (Da):38,193
Last modified:February 1, 1995 - v2
Checksum:iBF445C5E72FE2F94
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531L → F AA sequence (PubMed:1420277)Curated
Sequence conflicti180 – 1801E → S AA sequence (PubMed:1420277)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98458 Genomic DNA. Translation: AAA16427.1.
PIRiJN0575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98458 Genomic DNA. Translation: AAA16427.1 .
PIRi JN0575.

3D structure databases

ProteinModelPortali P29417.
SMRi P29417. Positions 30-325.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.
mycoCLAPi XYN10P_PENCH.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiXYNA_PENCH
AccessioniPrimary (citable) accession number: P29417
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3