[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Race 1 / Isolate SB111; PubMed=8400376 [NCBI, ExPASy, EBI, Israel, Japan] Apel P.C., Panaccione D.G., Holden F.R., Walton J.D.; "Cloning and targeted gene disruption of XYL1, a beta 1,4-xylanase gene from the maize pathogen Cochliobolus carbonum."; Mol. Plant Microbe Interact. 6:467-473(1993).
[2]	PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0885-5765(92)90070-C; AGRICOLA=IND92046127 Holden F.R., Walton J.D.; "Xylanases from the fungal maize pathogen Cochliobolus carbonum."; Physiol. Mol. Plant Pathol. 40:39-47(1992).

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.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L13596; AAA33024.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

O43097; 1YNA. [HSSP ENTRY / PDB]

SMR

Q06562; 31-218.

ModBase

Q06562.

Protein family/group databases

CAZy

GH11; Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA

3.2.1.8; 97658.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031176;	Molecular function: endo-1,4-beta-xylanase activity (inferred from electronic annotation from EC).
GO:0045493;	Biological process: xylan catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001137; Glyco_hydro_11.
IPR013319; Glyco_hydro_11/12_cat.
IPR018208; Glyco_hydro_11_AS.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.180; Glyco_hydro_11/12_cat; 1.

Pfam

PF00457; Glyco_hydro_11; 1.
Pfam graphical view of domain structure.

PRINTS

PR00911; GLHYDRLASE11.

PROSITE

PS00776; GLYCOSYL_HYDROL_F11_1; 1.
PS00777; GLYCOSYL_HYDROL_F11_2; 1.

Other

ProtoNet

Q06562.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal; Xylan degradation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`	`Potential.`
`CHAIN`	`31 221`	`191`	`Endo-1,4-beta-xylanase I.`	`PRO_0000008003`
`ACT_SITE`	`115 115`		`Nucleophile (By similarity).`
`ACT_SITE`	`206 206`		`Proton donor (By similarity).`
`CONFLICT`	`81 81`		`W -> I (in Ref. 2; AA sequence).`
`CONFLICT`	`107 107`		`G -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`131 131`		`S -> W (in Ref. 2; AA sequence).`

Sequence information

Length: 221 AA [This is the length of the unprocessed precursor]

Molecular weight: 23728 Da [This is the MW of the unprocessed precursor]

CRC64: 59DBD8983FC5B08C [This is a checksum on the sequence]

        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

Q06562 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools