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P40942

- CEXY_CLOSR

UniProt

P40942 - CEXY_CLOSR

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Protein
Thermostable celloxylanase
Gene
xynB
Organism
Clostridium stercorarium
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Proton donor By similarity
Active sitei293 – 2931Nucleophile By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. xylan catabolic process Source: UniProtKB-UniPathway
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 celloxylanase
PRO_0000184061Add
BLAST

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP40942.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
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

MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA    50
FRDYFPIGAA IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ 100
WADADRIVQF AKENGMELRF HTLVWHNQTP TGFSLDKEGK PMVEETDPQK 150
REENRKLLLQ RLENYIRAVV LRYKDDIKSW DVVNEVIEPN DPGGMRNSPW 200
YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD ILYELVKNLL 250
EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS 300
WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS 350
WLNGFPVKRT NAPLLFDRNF MPKPAFWAIV DPSRLRE 387
Length:387
Mass (Da):44,378
Last modified:February 1, 1995 - v1
Checksum:iC7221BD5E32C8E48
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12504 Genomic DNA. Translation: BAA02069.1.
PIRiJC2484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12504 Genomic DNA. Translation: BAA02069.1 .
PIRi JC2484.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DEP X-ray 1.80 A/B 41-387 [» ]
ProteinModelPortali P40942.
SMRi P40942. Positions 43-382.
ModBasei Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Miscellaneous databases

EvolutionaryTracei P40942.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
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. 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

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