Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q06562 (XYN1_COCCA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase I

Short name=Xylanase I
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 1
Gene names
Name:XYL1
OrganismCochliobolus carbonum (Bipolaris zeicola)
Taxonomic identifier5017 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major xylan-degrading enzyme. Contributes to the hydrolysis of arabinoxylan, the major component of maize cell-walls.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 221191Endo-1,4-beta-xylanase I
PRO_0000008003

Sites

Active site1151Nucleophile By similarity
Active site2061Proton donor By similarity

Experimental info

Sequence conflict811W → I AA sequence Ref.2
Sequence conflict1071G → A AA sequence Ref.2
Sequence conflict1311S → W AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06562 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 59DBD8983FC5B08C

FASTA22123,728
        10         20         30         40         50         60 
MVSFTSIITA AVAATGALAA PATDVSLVAR QNTPNGEGTH NGCFWSWWSD GGARATYTNG 

        70         80         90        100        110        120 
AGGSYSVSWG SGGNLVGGKG WNPGTARTIT YSGTYNYNGN SYLAVYGWTR NPLVEYYVVE 

       130        140        150        160        170        180 
NFGTYDPSSQ SQNKGTVTSD GSSYKIAQST RTNQPSIDGT RTFQQYWSVR QNKRSSGSVN 

       190        200        210        220 
MKTHFDAWAS KGMNLGQHYY QIVATEGYFS TGNAQITVNC P 

« Hide

References

[1]"Cloning and targeted gene disruption of XYL1, a beta 1,4-xylanase gene from the maize pathogen Cochliobolus carbonum."
Apel P.C., Panaccione D.G., Holden F.R., Walton J.D.
Mol. Plant Microbe Interact. 6:467-473(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Race 1 / Isolate SB111.
[2]"Xylanases from the fungal maize pathogen Cochliobolus carbonum."
Holden F.R., Walton J.D.
Physiol. Mol. Plant Pathol. 40:39-47(1992) [AGRICOLA] [Europe PMC]
Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13596 Genomic DNA. Translation: AAA33024.1.

3D structure databases

ProteinModelPortalQ06562.
SMRQ06562. Positions 31-218.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_COCCA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.8. 1551.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYN1_COCCA
AccessionPrimary (citable) accession number: Q06562
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 22, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries