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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway:ixylan 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 sitei187 – 1871Proton donorBy similarity
Active sitei293 – 2931NucleophilePROSITE-ProRule annotation

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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 407379Endo-1,4-beta-xylanasePRO_0000007968Add
BLAST

Expressioni

Inductioni

By xylose.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 363Combined sources
Helixi42 – 443Combined sources
Helixi48 – 525Combined sources
Turni53 – 553Combined sources
Beta strandi57 – 626Combined sources
Helixi64 – 685Combined sources
Helixi70 – 7910Combined sources
Beta strandi81 – 877Combined sources
Helixi91 – 944Combined sources
Helixi104 – 11512Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi128 – 1303Combined sources
Helixi133 – 1364Combined sources
Beta strandi141 – 1433Combined sources
Helixi144 – 1463Combined sources
Helixi150 – 17526Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1877Combined sources
Beta strandi193 – 1953Combined sources
Helixi199 – 2046Combined sources
Helixi207 – 22014Combined sources
Beta strandi224 – 2318Combined sources
Helixi238 – 25114Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi267 – 2704Combined sources
Helixi272 – 28413Combined sources
Beta strandi288 – 2969Combined sources
Beta strandi306 – 3083Combined sources
Helixi309 – 3113Combined sources
Helixi314 – 33320Combined sources
Helixi335 – 3373Combined sources
Beta strandi338 – 34710Combined sources
Helixi352 – 3565Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi376 – 3794Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi394 – 3963Combined sources
Helixi398 – 4047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HIZX-ray2.40A29-407[»]
1R85X-ray1.45A29-407[»]
1R86X-ray1.80A29-407[»]
1R87X-ray1.67A29-407[»]
3MMDX-ray1.70A29-407[»]
4PRWX-ray1.80A29-407[»]
4PUDX-ray2.01A37-407[»]
4PUEX-ray2.20A37-407[»]
ProteinModelPortaliP40943.
SMRiP40943. Positions 33-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40943.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 406365GH10PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ
60 70 80 90 100
RYKNEFTIGA AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK
110 120 130 140 150
FNFEQADRIV KFAKANGMDI RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP
160 170 180 190 200
VKREQNKQLL LKRLETHIKT IVERYKDDIK YWDVVNEVVG DDGKLRNSPW
210 220 230 240 250
YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT ALYNLVKQLK
260 270 280 290 300
EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG
310 320 330 340 350
WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH
360 370 380 390 400
TWLDSRADVY YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY

WAIIDHK
Length:407
Mass (Da):46,763
Last modified:February 1, 1995 - v1
Checksum:iAD385C90B252B82A
GO

Sequence cautioni

The sequence ABI49951.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49951.1. Different initiation.
PIRiI40570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ABI49951.1. Different initiation.
PIRiI40570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HIZX-ray2.40A29-407[»]
1R85X-ray1.45A29-407[»]
1R86X-ray1.80A29-407[»]
1R87X-ray1.67A29-407[»]
3MMDX-ray1.70A29-407[»]
4PRWX-ray1.80A29-407[»]
4PUDX-ray2.01A37-407[»]
4PUEX-ray2.20A37-407[»]
ProteinModelPortaliP40943.
SMRiP40943. Positions 33-407.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Miscellaneous databases

EvolutionaryTraceiP40943.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase."
    Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.
    Appl. Environ. Microbiol. 60:1889-1896(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: T-6 / NCIMB 40221.
  2. "Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6."
    Khasin A., Alchanati I., Shoham Y.
    Appl. Environ. Microbiol. 59:1725-1730(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-73.
    Strain: T-6.

Entry informationi

Entry nameiXYN1_GEOSE
AccessioniPrimary (citable) accession number: P40943
Secondary accession number(s): Q09LX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 94 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, Direct protein sequencing

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

External Data

Dasty 3

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 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.