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Protein

Beta-xylosidase

Gene

xynB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei160Proton donorPROSITE-ProRule annotation1
Active sitei280NucleophileBy similarity1

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

BRENDAi3.2.1.37. 623.
SABIO-RKQ9ZFM2.

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
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000576871 – 504Beta-xylosidaseAdd BLAST504

Structurei

Secondary structure

1504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi11 – 13Combined sources3
Helixi17 – 19Combined sources3
Beta strandi20 – 23Combined sources4
Helixi27 – 31Combined sources5
Helixi33 – 45Combined sources13
Beta strandi49 – 52Combined sources4
Beta strandi56 – 58Combined sources3
Turni59 – 61Combined sources3
Beta strandi64 – 77Combined sources14
Helixi80 – 91Combined sources12
Beta strandi95 – 100Combined sources6
Helixi105 – 107Combined sources3
Beta strandi108 – 110Combined sources3
Turni115 – 118Combined sources4
Helixi127 – 145Combined sources19
Helixi147 – 151Combined sources5
Beta strandi153 – 157Combined sources5
Turni164 – 166Combined sources3
Helixi168 – 170Combined sources3
Helixi172 – 189Combined sources18
Beta strandi194 – 200Combined sources7
Helixi206 – 217Combined sources12
Beta strandi224 – 230Combined sources7
Beta strandi236 – 238Combined sources3
Helixi252 – 267Combined sources16
Beta strandi269 – 271Combined sources3
Beta strandi276 – 283Combined sources8
Helixi290 – 293Combined sources4
Helixi295 – 307Combined sources13
Helixi308 – 310Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi320 – 322Combined sources3
Beta strandi331 – 336Combined sources6
Beta strandi340 – 342Combined sources3
Helixi343 – 345Combined sources3
Helixi349 – 358Combined sources10
Beta strandi362 – 368Combined sources7
Beta strandi371 – 375Combined sources5
Beta strandi381 – 386Combined sources6
Beta strandi398 – 405Combined sources8
Beta strandi407 – 423Combined sources17
Helixi425 – 431Combined sources7
Helixi440 – 448Combined sources9
Beta strandi452 – 459Combined sources8
Helixi461 – 463Combined sources3
Beta strandi464 – 471Combined sources8
Beta strandi476 – 483Combined sources8
Helixi488 – 490Combined sources3
Helixi496 – 498Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W91X-ray2.20A/B/C/D/E/F/G/H1-504[»]
2BFGX-ray2.40A/B/C/D/E/F/G/H1-504[»]
2BS9X-ray2.20A/B/C/D/E/F/G/H1-504[»]
ProteinModelPortaliQ9ZFM2.
SMRiQ9ZFM2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZFM2.

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.

Q9ZFM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVNVPSNG REKFKKNWKF CVGTGRLGLA LQKEYLDHLK LVQEKIGFRY
60 70 80 90 100
IRGHGLLSDD VGIYREVEID GEMKPFYNFT YIDRIVDSYL ALNIRPFIEF
110 120 130 140 150
GFMPKALASG DQTVFYWKGN VTPPKDYNKW RDLIVAVVSH FIERYGIEEV
160 170 180 190 200
RTWLFEVWNE PNLVNFWKDA NKQEYFKLYE VTARAVKSVD PHLQVGGPAI
210 220 230 240 250
CGGSDEWITD FLHFCAERRV PVDFVSRHAY TSKAPHKKTF EYYYQELELE
260 270 280 290 300
PPEDMLEQFK TVRALIRQSP FPHLPLHITE YNTSYSPINP VHDTALNAAY
310 320 330 340 350
IARILSEGGD YVDSFSYWTF SDVFEEMDVP KALFHGGFGL VALHSIPKPT
360 370 380 390 400
FHAFTFFNAL GDELLYRDGE MIVTRRKDGS IAAVLWNLVM EKGEGLTKEV
410 420 430 440 450
QLVIPVSFSA VFIKRQIVNE QYGNAWRVWK QMGRPRFPSR QAVETLPSAQ
460 470 480 490 500
PHVMTEQRRA TDGVIHLSIV LSKNEVTLIE IEQVRDETST YVGLDDGEIT

SYSS
Length:504
Mass (Da):58,119
Last modified:May 1, 1999 - v1
Checksum:i59518E75200A18B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49941.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49941.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W91X-ray2.20A/B/C/D/E/F/G/H1-504[»]
2BFGX-ray2.40A/B/C/D/E/F/G/H1-504[»]
2BS9X-ray2.20A/B/C/D/E/F/G/H1-504[»]
ProteinModelPortaliQ9ZFM2.
SMRiQ9ZFM2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH39. Glycoside Hydrolase Family 39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.37. 623.
SABIO-RKQ9ZFM2.

Miscellaneous databases

EvolutionaryTraceiQ9ZFM2.

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_GEOSE
AccessioniPrimary (citable) accession number: Q9ZFM2
Secondary accession number(s): Q09LY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 71 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.