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Protein

Beta-xylosidase

Gene

xynB

Organism
Thermoanaerobacterium saccharolyticum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Temperature dependencei

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

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donorPROSITE-ProRule annotation
Active sitei277 – 2771Nucleophile1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

SABIO-RKP36906.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH39. Glycoside Hydrolase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylosidase (EC:3.2.1.37)
Alternative name(s):
1,4-beta-D-xylan xylohydrolase
Xylan 1,4-beta-xylosidase
Gene namesi
Name:xynB
OrganismiThermoanaerobacterium saccharolyticum
Taxonomic identifieri28896 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Beta-xylosidasePRO_0000057689Add
BLAST

Expressioni

Inductioni

By xylan and xylose.

Interactioni

Chemistry

BindingDBiP36906.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi17 – 193Combined sources
Beta strandi20 – 234Combined sources
Helixi27 – 315Combined sources
Helixi33 – 4311Combined sources
Beta strandi50 – 523Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 776Combined sources
Helixi80 – 9213Combined sources
Beta strandi98 – 1003Combined sources
Turni105 – 1073Combined sources
Beta strandi108 – 1103Combined sources
Turni115 – 1184Combined sources
Helixi127 – 14519Combined sources
Helixi147 – 1504Combined sources
Beta strandi155 – 1595Combined sources
Turni164 – 1663Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 18918Combined sources
Beta strandi195 – 2006Combined sources
Helixi206 – 21813Combined sources
Beta strandi223 – 2308Combined sources
Helixi249 – 26416Combined sources
Beta strandi273 – 2808Combined sources
Helixi287 – 2904Combined sources
Helixi292 – 30413Combined sources
Helixi305 – 3073Combined sources
Beta strandi310 – 3156Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi337 – 3393Combined sources
Turni340 – 3423Combined sources
Helixi346 – 3549Combined sources
Beta strandi359 – 3657Combined sources
Beta strandi368 – 3725Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi395 – 4028Combined sources
Beta strandi404 – 42017Combined sources
Helixi422 – 4287Combined sources
Helixi437 – 44610Combined sources
Beta strandi450 – 4545Combined sources
Beta strandi462 – 4698Combined sources
Beta strandi473 – 4819Combined sources
Helixi486 – 4883Combined sources
Helixi494 – 4963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PX8X-ray2.40A/B1-500[»]
1UHVX-ray2.10A/B/C/D1-500[»]
ProteinModelPortaliP36906.
SMRiP36906. Positions 1-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36906.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 39 family.Curated

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSiPR00745. GLHYDRLASE39.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKVRVPDFS DKKFSDRWRY CVGTGRLGLA LQKEYIETLK YVKENIDFKY
60 70 80 90 100
IRGHGLLCDD VGIYREDVVG DEVKPFYNFT YIDRIFDSFL EIGIRPFVEI
110 120 130 140 150
GFMPKKLASG TQTVFYWEGN VTPPKDYEKW SDLVKAVLHH FISRYGIEEV
160 170 180 190 200
LKWPFEIWNE PNLKEFWKDA DEKEYFKLYK VTAKAIKEVN ENLKVGGPAI
210 220 230 240 250
CGGADYWIED FLNFCYEENV PVDFVSRHAT TSKQGEYTPH LIYQEIMPSE
260 270 280 290 300
YMLNEFKTVR EIIKNSHFPN LPFHITEYNT SYSPQNPVHD TPFNAAYIAR
310 320 330 340 350
ILSEGGDYVD SFSYWTFSDV FEERDVPRSQ FHGGFGLVAL NMIPKPTFYT
360 370 380 390 400
FKFFNAMGEE MLYRDEHMLV TRRDDGSVAL IAWNEVMDKT ENPDEDYEVE
410 420 430 440 450
IPVRFRDVFI KRQLIDEEHG NPWGTWIHMG RPRYPSKEQV NTLREVAKPE
460 470 480 490 500
IMTSQPVAND GYLNLKFKLG KNAVVLYELT ERIDESSTYI GLDDSKINGY
Length:500
Mass (Da):58,606
Last modified:June 1, 1994 - v1
Checksum:i3B6D59E70A5F4CBC
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97883 Genomic DNA. Translation: AAA27369.1.
PIRiS41859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97883 Genomic DNA. Translation: AAA27369.1.
PIRiS41859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PX8X-ray2.40A/B1-500[»]
1UHVX-ray2.10A/B/C/D1-500[»]
ProteinModelPortaliP36906.
SMRiP36906. Positions 1-500.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP36906.
ChEMBLiCHEMBL4658.

Protein family/group databases

CAZyiGH39. Glycoside Hydrolase Family 39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
SABIO-RKP36906.

Miscellaneous databases

EvolutionaryTraceiP36906.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSiPR00745. GLHYDRLASE39.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 49915 / DSM 7060 / 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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 49915 / DSM 7060 / 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] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE GLU-277, MASS SPECTROMETRY.

Entry informationi

Entry nameiXYNB_THESA
AccessioniPrimary (citable) accession number: P36906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 14, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.