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Protein

Endo-1,4-beta-xylanase

Gene

xynB

Organism
Dictyoglomus thermophilum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotationImported

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_DICTH.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xynBImported
OrganismiDictyoglomus thermophilumImported
Taxonomic identifieri14 [NCBI]
Taxonomic lineageiBacteriaDictyoglomiDictyoglomalesDictyoglomaceaeDictyoglomus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 360336Endo-1,4-beta-xylanaseSequence analysisPRO_5004161676Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi309799.DICTH_1968.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5JX-ray1.80A/B30-225[»]
ProteinModelPortaliP77853.
SMRiP77853. Positions 30-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77853.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 221193GH11 (glycosyl hydrolase family 11)InterPro annotationAdd
BLAST
Domaini242 – 360119CBM6 (carbohydrate binding type-6)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77853-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKKLSKLL LVVLLVAVYT QVNAQTSITL TSNASGTFDG YYYELWKDTG
60 70 80 90 100
NTTMTVYTQG RFSCQWSNIN NALFRTGKKY NQNWQSLGTI RITYSATYNP
110 120 130 140 150
NGNSYLCIYG WSTNPLVEFY IVESWGNWRP PGATSLGQVT IDGGTYDIYR
160 170 180 190 200
TTRVNQPSIV GTATFDQYWS VRTSKRTSGT VTVTDHFRAW ANRGLNLGTI
210 220 230 240 250
DQITLCVEGY QSSGSANITQ NTFSQGSSSG SSGGSSGSTT TTRIECENMS
260 270 280 290 300
LSGPYVSRIT NPFNGIALYA NGDTARATVN FPASRNYNFR LRGCGNNNNL
310 320 330 340 350
ARVDLRIDGR TVGTFYYQGT YPWEAPIDNV YVSAGSHTVE ITVTADNGTW
360
DVYADYLVIQ
Length:360
Mass (Da):39,788
Last modified:February 1, 1997 - v1
Checksum:iC7909E007FA58AEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76545 Genomic DNA. Translation: AAC46361.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76545 Genomic DNA. Translation: AAC46361.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5JX-ray1.80A/B30-225[»]
ProteinModelPortaliP77853.
SMRiP77853. Positions 30-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309799.DICTH_1968.

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_DICTH.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.

Miscellaneous databases

EvolutionaryTraceiP77853.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the xynB gene from Dictyoglomus thermophilum Rt46B.1 and action of the gene product on kraft pulp."
    Morris D.D., Gibbs M.D., Chin C.W., Koh M.H., Wong K.K., Allison R.W., Nelson P.J., Bergquist P.L.
    Appl. Environ. Microbiol. 64:1759-1765(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Rt46B.1Imported.
  2. "Structure of XynB, a highly thermostable beta-1,4-xylanase from Dictyoglomus thermophilum Rt46B.1, at 1.8 A resolution."
    McCarthy A.A., Morris D.D., Bergquist P.L., Baker E.N.
    Acta Crystallogr. D 56:1367-1375(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 30-225.

Entry informationi

Entry nameiP77853_DICTH
AccessioniPrimary (citable) accession number: P77853
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.