Endo-1,4-beta-xylanase precursor - Thermopolyspora flexuosa

Preferred order of sections

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase RuleBase RU004392
EC=3.2.1.8 RuleBase RU004392

Gene names

Name:

xyn11A EMBL CAD48747.1

Organism

Thermopolyspora flexuosa EMBL CAD48747.1

Taxonomic identifier

103836 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Streptosporangiaceae › Thermopolyspora

Protein attributes

Sequence length	344 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)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392
Pathway	Glycan degradation; xylan degradation. RuleBase RU004392
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433

Ontologies

Keywords
Biological process	Xylan degradation RuleBase RU003433 EMBL CAD48747.1
Domain	Signal EMBL CAD48747.1
Molecular function	Glycosidase RuleBase RU003433 Hydrolase
Technical term	3D-structure PDB 1M4W PDB 3MFA PDB 3MFC PDB 3MF9 PDB 3MF6
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 43

43

EMBL CAD48747.1

Chain

44 – 344

301

endoxylanase EMBL CAD48747.1

PRO_5000068863

Amino acid modifications

Glycosylation

50

1

N-linked (GlcNAc...) PDB 1M4W

Sequences

Sequence

Length

Mass (Da)

Tools

Q8GMV7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E4BC3FFAD095AA02
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FASTA

344

37,497

        10         20         30         40         50         60 
MNEPLTITQA RRRRRLGLRR IVTSAFALAL AIAGALLPGT AHADTTITQN QTGYDNGYFY 

        70         80         90        100        110        120 
SFWTDAPGTV SMTLHSGGSY STSWRNTGNF VAGKGWSTGG RRTVTYNASF NPSGNAYLTL 

       130        140        150        160        170        180 
YGWTRNPLVE YYIVESWGTY RPTGTYKGTV TTDGGTYDIY ETWRYNAPSI EGTRTFQQFW 

       190        200        210        220        230        240 
SVRQQKRTSG TITIGNHFDA WARAGMNLGS HDYQIMATEG YQSSGSSTVS ISEGGNPGNP 

       250        260        270        280        290        300 
GNPGNPGNPG NPGNPGGGCV ATLSAGQQWS DRYNLNVSVS GSNNWTVRMD VPYPARIIAT 

       310        320        330        340 
WNIHAQWPES QVLIARPNGN GNNWGVTIQH NGNWTWPTVT CTAN

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References

[1]	"Thermostable xylanases, Xyn10A and Xyn11A, from the actinomycete Nonomuraea flexuosa: isolation of the genes and characterization of recombinant Xyn11A polypeptides produced in Trichoderma reesei." Leskinen S., Mantyla A., Fagerstrom R., Vehmaanpera J., Lantto R., Paloheimo M., Suominen P. Appl. Microbiol. Biotechnol. 67:495-505(2005) [PubMed: 15650852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability." Hakulinen N., Turunen O., Janis J., Leisola M., Rouvinen J. Eur. J. Biochem. 270:1399-1412(2003) [PubMed: 12653995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 44-240, GLYCOSYLATION AT ASN-50.
[3]	"Computational design of an endo-1,4-{beta}-xylanase ligand binding site." Morin A., Kaufmann K.W., Fortenberry C., Harp J.M., Mizoue L.S., Meiler J. Protein Eng. Des. Sel. 0:0-0(2011) [PubMed: 21349882] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 44-234.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ508952 Genomic DNA. Translation: CAD48747.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M4W	X-ray	2.10	A	44-240	[»]
3MF6	X-ray	1.28	A	44-234	[»]
3MF9	X-ray	1.70	A	44-234	[»]
3MFA	X-ray	1.63	A	44-235	[»]
3MFC	X-ray	1.70	A	44-235	[»]

ProteinModelPortal

Q8GMV7.

SMR

Q8GMV7. Positions 44-240.

ModBase

Search...

Protein family/group databases

CAZy

CBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]

Gene3D

G3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

SMART

SM00637. CBD_II. 1 hit.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS51173. CBM2. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q8GMV7_9ACTO

Accession

Primary (citable) accession number: Q8GMV7

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)