Alkaline thermostable endoxylanase precursor

Preferred order of sections

Names and origin

Protein names	Submitted name: Alkaline thermostable endoxylanase EMBL AAB70918.1 EC=3.2.1.8 EMBL AAB70918.1
Organism	Bacillus sp. NG-27 EMBL AAB70918.1
Taxonomic identifier	65673 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	405 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)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432

Ontologies

Keywords
Biological process	Xylan degradation EMBL AAB70918.1
Domain	Signal EMBL AAB70918.1
Ligand	Magnesium PDB 2FGL PDB 2F8Q Metal-binding PDB 2FGL PDB 2F8Q
Molecular function	Glycosidase RuleBase RU003432 EMBL AAB70918.1 Hydrolase
Technical term	3D-structure PDB 2FGL PDB 2F8Q
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential EMBL AAB70918.1

Chain

29 – 405

377

Potential EMBL AAB70918.1

PRO_5000053362

Sites

Metal binding

69

1

Magnesium; via carbonyl oxygen PDB 2FGL

Metal binding

353

1

Magnesium; via carbonyl oxygen PDB 2FGL

Metal binding

356

1

Magnesium; via carbonyl oxygen PDB 2FGL

Sequences

Sequence

Length

Mass (Da)

Tools

O30700 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B081CB2FF8BFFCE2
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FASTA

405

46,021

        10         20         30         40         50         60 
MLKTLRKPFI AGLALSLLLT GGASSVFAQG NGQAGPPKGG IFKEGEKGNG NVQPFAWQVA 

        70         80         90        100        110        120 
SLADRYEESF DIGAAVEPHQ LNGRQGKVLK HHYNSIVAEN AMKPISLQPE EGVFTWDGAD 

       130        140        150        160        170        180 
AIVEFARKNN MNLRFHTLVW HNQVPDWFFL DEEGNPMVEE TNEAKRQANK ELLLERLETH 

       190        200        210        220        230        240 
IKTVVERYKD DVTAWDVVNE VVDDGTPNER GLRESVWYQI TGDEYIRVAF ETARKYAGED 

       250        260        270        280        290        300 
AKLFINDYNT EVTPKRDHLY NLVQDLLADG VPIDGVGHQA HIQIDWPTID EIRTSMEMFA 

       310        320        330        340        350        360 
GLGLDNQVTE LDVSLYGWPP RPAFPTYDAI PQERFQAQAD RYNQLFELYE ELDADLSSVT 

       370        380        390        400 
FWGIADNHTW LDDRAREYND GVGKDAPFVF DPNYRVKPAF WRIID

« Hide

References

[1]	"Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus sp. Strain NG-27." Gupta N., Reddy V.S., Maiti S., Ghosh A. Appl. Environ. Microbiol. 66:2631-2635(2000) [PubMed: 10831448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: NG-27 EMBL AAB70918.1.
[2]	"Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditions." Manikandan K., Bhardwaj A., Gupta N., Lokanath N.K., Ghosh A., Reddy V.S., Ramakumar S. Protein Sci. 15:1951-1960(2006) [PubMed: 16823036] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 52-405 IN COMPLEX WITH MAGNESIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF015445 Genomic DNA. Translation: AAB70918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F8Q	X-ray	2.20	A/B	53-405	[»]
2FGL	X-ray	2.20	A/B	52-405	[»]

ProteinModelPortal

O30700.

SMR

O30700. Positions 52-405.

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O30700_9BACI

Accession

Primary (citable) accession number: O30700

Entry history

Integrated into UniProtKB/TrEMBL:	January 1, 1998
Last sequence update:	January 1, 1998
Last modified:	May 31, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)