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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donorPROSITE-ProRule annotation
Active sitei280 – 2801NucleophileBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Beta-xylosidasePRO_0000057687Add
BLAST

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi11 – 133Combined sources
Helixi17 – 193Combined sources
Beta strandi20 – 234Combined sources
Helixi27 – 315Combined sources
Helixi33 – 4513Combined sources
Beta strandi49 – 524Combined sources
Beta strandi56 – 583Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 7714Combined sources
Helixi80 – 9112Combined sources
Beta strandi95 – 1006Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 1103Combined sources
Turni115 – 1184Combined sources
Helixi127 – 14519Combined sources
Helixi147 – 1515Combined sources
Beta strandi153 – 1575Combined sources
Turni164 – 1663Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 18918Combined sources
Beta strandi194 – 2007Combined sources
Helixi206 – 21712Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi236 – 2383Combined sources
Helixi252 – 26716Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi276 – 2838Combined sources
Helixi290 – 2934Combined sources
Helixi295 – 30713Combined sources
Helixi308 – 3103Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi340 – 3423Combined sources
Helixi343 – 3453Combined sources
Helixi349 – 35810Combined sources
Beta strandi362 – 3687Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi381 – 3866Combined sources
Beta strandi398 – 4058Combined sources
Beta strandi407 – 42317Combined sources
Helixi425 – 4317Combined sources
Helixi440 – 4489Combined sources
Beta strandi452 – 4598Combined sources
Helixi461 – 4633Combined sources
Beta strandi464 – 4718Combined sources
Beta strandi476 – 4838Combined sources
Helixi488 – 4903Combined sources
Helixi496 – 4983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-503.
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
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. Positions 4-503.
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...

Publicationsi

  1. "The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6."
    Shulami S., Gat O., Sonenshein A.L., Shoham Y.
    J. Bacteriol. 181:3695-3704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: T-6.

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: October 14, 2015
This is version 69 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.