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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotationImported

Enzyme and pathway databases

BRENDAi3.2.1.8. 6298.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
OrganismiThermobifida fusca (Thermomonospora fusca)Imported
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Sequence analysisAdd
BLAST
Chaini43 – 338296Endo-1,4-beta-xylanaseSequence analysisPRO_5004250896Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_1213.

Structurei

3D structure databases

ProteinModelPortaliQ56265.
SMRiQ56265. Positions 44-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 229187GH11 (glycosyl hydrolase family 11)InterPro annotationAdd
BLAST
Domaini246 – 33893CBM2 (carbohydrate binding type-2)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.
OrthoDBiEOG63VBWG.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHAPASLKS RRRFRPRLLI GKAFAAALVA VVTMIPSTAA HAAVTSNETG
60 70 80 90 100
YHDGYFYSFW TDAPGTVSME LGPGGNYSTS WRNTGNFVAG KGWATGGRRT
110 120 130 140 150
VTYSASFNPS GNAYLTLYGW TRNPLVEYYI VESWGTYRPT GTYMGTVTTD
160 170 180 190 200
GGTYDIYKTT RYNAPSIEGT RTFDQYWSVR QSKRTSGTIT AGNHFDAWAR
210 220 230 240 250
HGMHLGTHDY MIMATEGYQS SGSSNVTLGT SGGGNPGGGN PPGGGNPPGG
260 270 280 290 300
GGCTATLSAG QQWNDRYNLN VNVSGSNNWT VTVNVPWPAR IIATWNIHAS
310 320 330
YPDSQTLVAR PNGNGNNWGM TIMHNGNWTW PTVSCSAN
Length:338
Mass (Da):36,406
Last modified:November 1, 1996 - v1
Checksum:i188AF3AA8430A3C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01242 Genomic DNA. Translation: AAA21480.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01242 Genomic DNA. Translation: AAA21480.1.

3D structure databases

ProteinModelPortaliQ56265.
SMRiQ56265. Positions 44-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_1213.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.
OrthoDBiEOG63VBWG.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6298.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of a Thermomonospora fusca xylanase gene and its expression in Escherichia coli and Streptomyces lividans."
    Ghangas G.S., Hu Y.J., Wilson D.B.
    J. Bacteriol. 171:2963-2969(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: YXImported.
  2. "Characterization and sequence of a Thermomonospora fusca xylanase."
    Irwin D., Jung E.D., Wilson D.B.
    Appl. Environ. Microbiol. 60:763-770(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: YXImported.

Entry informationi

Entry nameiQ56265_THEFU
AccessioniPrimary (citable) accession number: Q56265
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.