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Protein

Thermostable celloxylanase

Gene

xynB

Organism
Clostridium stercorarium
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Active toward xylan, carboxymethylcellulose, P-nitrophenyl-beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

pH dependencei

Optimum pH is 7.0.

Temperature dependencei

Optimum temperature is 80 degrees Celsius.

Pathway: 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 sitei185 – 1851Proton 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, Cellulose degradation, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermostable celloxylanase (EC:3.2.1.4, EC:3.2.1.8)
Gene namesi
Name:xynB
OrganismiClostridium stercorarium
Taxonomic identifieri1510 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Thermostable celloxylanasePRO_0000184061Add
BLAST

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 504Combined sources
Turni51 – 544Combined sources
Beta strandi57 – 615Combined sources
Helixi63 – 653Combined sources
Helixi68 – 7710Combined sources
Beta strandi79 – 857Combined sources
Helixi89 – 924Combined sources
Helixi102 – 11312Combined sources
Beta strandi117 – 12812Combined sources
Helixi131 – 1344Combined sources
Beta strandi139 – 1413Combined sources
Helixi142 – 1443Combined sources
Helixi148 – 17326Combined sources
Turni174 – 1763Combined sources
Beta strandi179 – 1846Combined sources
Helixi192 – 1943Combined sources
Helixi199 – 2046Combined sources
Helixi207 – 22014Combined sources
Beta strandi222 – 23110Combined sources
Helixi236 – 25116Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2685Combined sources
Helixi272 – 28312Combined sources
Turni284 – 2863Combined sources
Beta strandi288 – 29912Combined sources
Helixi313 – 33119Combined sources
Helixi332 – 3365Combined sources
Beta strandi337 – 3437Combined sources
Helixi351 – 3533Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi364 – 3663Combined sources
Helixi374 – 3807Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DEPX-ray1.80A/B41-387[»]
ProteinModelPortaliP40942.
SMRiP40942. Positions 43-382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40942.

Family & Domainsi

Sequence similaritiesi

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. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA
60 70 80 90 100
FRDYFPIGAA IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ
110 120 130 140 150
WADADRIVQF AKENGMELRF HTLVWHNQTP TGFSLDKEGK PMVEETDPQK
160 170 180 190 200
REENRKLLLQ RLENYIRAVV LRYKDDIKSW DVVNEVIEPN DPGGMRNSPW
210 220 230 240 250
YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD ILYELVKNLL
260 270 280 290 300
EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS
310 320 330 340 350
WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS
360 370 380
WLNGFPVKRT NAPLLFDRNF MPKPAFWAIV DPSRLRE
Length:387
Mass (Da):44,378
Last modified:February 1, 1995 - v1
Checksum:iC7221BD5E32C8E48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12504 Genomic DNA. Translation: BAA02069.1.
PIRiJC2484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12504 Genomic DNA. Translation: BAA02069.1.
PIRiJC2484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DEPX-ray1.80A/B41-387[»]
ProteinModelPortaliP40942.
SMRiP40942. Positions 43-382.
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

EvolutionaryTraceiP40942.

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. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase, and characterization of the translated product."
    Fukumura M., Sakka K., Shimada K., Ohmiya K.
    Biosci. Biotechnol. Biochem. 59:40-46(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: F-9.

Entry informationi

Entry nameiCEXY_CLOSR
AccessioniPrimary (citable) accession number: P40942
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 74 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

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.