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P36906 (XYNB_THESA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-xylosidase
EC=3.2.1.37
Alternative name(s):
1,4-beta-D-xylan xylohydrolase
Xylan 1,4-beta-xylosidase
Gene names
Name:xynB
OrganismThermoanaerobacter saccharolyticum
Taxonomic identifier28896 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has hydrolytic activity towards xylopentaose, xylotriose, xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity toward xylan.

Catalytic activity

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.

Pathway

Glycan degradation; xylan degradation.

Induction

By xylan and xylose.

Sequence similarities

Belongs to the glycosyl hydrolase 39 family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Loses activity at 85 degrees Celsius.

Mass spectrometry

Molecular mass is 58666±6 Da from positions 1 - 500. Determined by ESI. Ref.3

Ontologies

Keywords
   Biological processXylan degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

xylan 1,4-beta-xylosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Beta-xylosidase
PRO_0000057689

Sites

Active site1601Proton donor Potential
Active site2771Nucleophile Ref.3

Secondary structure

1 ...................................................................................... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36906 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3B6D59E70A5F4CBC

FASTA50058,606
        10         20         30         40         50         60 
MIKVRVPDFS DKKFSDRWRY CVGTGRLGLA LQKEYIETLK YVKENIDFKY IRGHGLLCDD 

        70         80         90        100        110        120 
VGIYREDVVG DEVKPFYNFT YIDRIFDSFL EIGIRPFVEI GFMPKKLASG TQTVFYWEGN 

       130        140        150        160        170        180 
VTPPKDYEKW SDLVKAVLHH FISRYGIEEV LKWPFEIWNE PNLKEFWKDA DEKEYFKLYK 

       190        200        210        220        230        240 
VTAKAIKEVN ENLKVGGPAI CGGADYWIED FLNFCYEENV PVDFVSRHAT TSKQGEYTPH 

       250        260        270        280        290        300 
LIYQEIMPSE YMLNEFKTVR EIIKNSHFPN LPFHITEYNT SYSPQNPVHD TPFNAAYIAR 

       310        320        330        340        350        360 
ILSEGGDYVD SFSYWTFSDV FEERDVPRSQ FHGGFGLVAL NMIPKPTFYT FKFFNAMGEE 

       370        380        390        400        410        420 
MLYRDEHMLV TRRDDGSVAL IAWNEVMDKT ENPDEDYEVE IPVRFRDVFI KRQLIDEEHG 

       430        440        450        460        470        480 
NPWGTWIHMG RPRYPSKEQV NTLREVAKPE IMTSQPVAND GYLNLKFKLG KNAVVLYELT 

       490        500 
ERIDESSTYI GLDDSKINGY

« Hide

References

[1]"Genetic organization, sequence and biochemical characterization of recombinant beta-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI."
Lee Y.E., Zeikus J.G.
J. Gen. Microbiol. 139:1235-1243(1993) [PubMed: 8360617] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B6A-RI.
[2]"Stereochemical course and reaction products of the action of beta-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI."
Armand S., Vieille C., Gey C., Heyraud A., Zeikus J.G., Henrissat B.
Eur. J. Biochem. 236:706-713(1996) [PubMed: 8612648] [Abstract]
Cited for: CHARACTERIZATION.
Strain: B6A-RI.
[3]"Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum beta-xylosidase using electrospray MS."
Vocadlo D.J., MacKenzie L.F., He S., Zeikus G.J., Withers S.G.
Biochem. J. 335:449-455(1998) [PubMed: 9761746] [Abstract]
Cited for: ACTIVE SITE GLU-277, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M97883 Genomic DNA. Translation: AAA27369.1.
PIRS41859.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PX8X-ray2.40A/B1-500[»]
1UHVX-ray2.10A/B/C/D1-500[»]
ProteinModelPortalP36906.
SMRP36906. Positions 1-500.
ModBaseSearch...

Protein family/group databases

CAZyGH39. Glycoside Hydrolase Family 39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSPR00745. GLHYDRLASE39.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_THESA
AccessionPrimary (citable) accession number: P36906
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 31, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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