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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)DescriptionActionsGraphical viewLength
Active sitei160Proton donorPROSITE-ProRule annotation1
Active sitei277Nucleophile1 Publication1

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 databases

ChEMBLiCHEMBL4658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000576891 – 500Beta-xylosidaseAdd BLAST500

Expressioni

Inductioni

By xylan and xylose.

Interactioni

Chemistry databases

BindingDBiP36906.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi17 – 19Combined sources3
Beta strandi20 – 23Combined sources4
Helixi27 – 31Combined sources5
Helixi33 – 43Combined sources11
Beta strandi50 – 52Combined sources3
Turni59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 77Combined sources6
Helixi80 – 92Combined sources13
Beta strandi98 – 100Combined sources3
Turni105 – 107Combined sources3
Beta strandi108 – 110Combined sources3
Turni115 – 118Combined sources4
Helixi127 – 145Combined sources19
Helixi147 – 150Combined sources4
Beta strandi155 – 159Combined sources5
Turni164 – 166Combined sources3
Helixi168 – 170Combined sources3
Helixi172 – 189Combined sources18
Beta strandi195 – 200Combined sources6
Helixi206 – 218Combined sources13
Beta strandi223 – 230Combined sources8
Helixi249 – 264Combined sources16
Beta strandi273 – 280Combined sources8
Helixi287 – 290Combined sources4
Helixi292 – 304Combined sources13
Helixi305 – 307Combined sources3
Beta strandi310 – 315Combined sources6
Beta strandi317 – 319Combined sources3
Beta strandi337 – 339Combined sources3
Turni340 – 342Combined sources3
Helixi346 – 354Combined sources9
Beta strandi359 – 365Combined sources7
Beta strandi368 – 372Combined sources5
Beta strandi378 – 384Combined sources7
Beta strandi395 – 402Combined sources8
Beta strandi404 – 420Combined sources17
Helixi422 – 428Combined sources7
Helixi437 – 446Combined sources10
Beta strandi450 – 454Combined sources5
Beta strandi462 – 469Combined sources8
Beta strandi473 – 481Combined sources9
Helixi486 – 488Combined sources3
Helixi494 – 496Combined sources3

3D structure databases

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

Chemistry databases

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...

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: November 2, 2016
This is version 88 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.