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Protein

Endo-1,4-beta-xylanase I

Gene

XYL1

Organism
Cochliobolus carbonum (Bipolaris zeicola)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151NucleophilePROSITE-ProRule annotation
Active sitei206 – 2061Proton donorPROSITE-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

BRENDAi3.2.1.8. 1551.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_COCCA.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase I (EC:3.2.1.8)
Short name:
Xylanase I
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 1
Gene namesi
Name:XYL1
OrganismiCochliobolus carbonum (Bipolaris zeicola)
Taxonomic identifieri5017 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 221191Endo-1,4-beta-xylanase IPRO_0000008003Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Structurei

3D structure databases

ProteinModelPortaliQ06562.
SMRiQ06562. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFTSIITA AVAATGALAA PATDVSLVAR QNTPNGEGTH NGCFWSWWSD
60 70 80 90 100
GGARATYTNG AGGSYSVSWG SGGNLVGGKG WNPGTARTIT YSGTYNYNGN
110 120 130 140 150
SYLAVYGWTR NPLVEYYVVE NFGTYDPSSQ SQNKGTVTSD GSSYKIAQST
160 170 180 190 200
RTNQPSIDGT RTFQQYWSVR QNKRSSGSVN MKTHFDAWAS KGMNLGQHYY
210 220
QIVATEGYFS TGNAQITVNC P
Length:221
Mass (Da):23,728
Last modified:February 1, 1995 - v1
Checksum:i59DBD8983FC5B08C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811W → I AA sequence (Ref. 2) Curated
Sequence conflicti107 – 1071G → A AA sequence (Ref. 2) Curated
Sequence conflicti131 – 1311S → W AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13596 Genomic DNA. Translation: AAA33024.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13596 Genomic DNA. Translation: AAA33024.1.

3D structure databases

ProteinModelPortaliQ06562.
SMRiQ06562. Positions 31-218.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_COCCA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 1551.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiXYN1_COCCA
AccessioniPrimary (citable) accession number: Q06562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 79 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.