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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.PROSITE-ProRule annotation
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)DescriptionActionsGraphical viewLength
Active sitei127NucleophilePROSITE-ProRule annotation1
Active sitei216Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidasePROSITE-ProRule annotation, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradationPROSITE-ProRule 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-xylanasePROSITE-ProRule annotation (EC:3.2.1.8PROSITE-ProRule annotation)
OrganismiThermobifida fusca (Thermomonospora fusca)Imported
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Sequence analysisAdd BLAST42
ChainiPRO_500425089643 – 338Endo-1,4-beta-xylanaseSequence analysisAdd BLAST296

Interactioni

Protein-protein interaction databases

STRINGi269800.Tfu_1213.

Structurei

3D structure databases

ProteinModelPortaliQ56265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 229GH11 (glycosyl hydrolase family 11)InterPro annotationAdd BLAST187
Domaini246 – 338CBM2 (carbohydrate binding type-2)InterPro annotationAdd BLAST93

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.PROSITE-ProRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.40.290. 1 hit.
InterProiView protein in InterPro
IPR008965. 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.
PfamiView protein in Pfam
PF00457. Glyco_hydro_11. 1 hit.
PRINTSiPR00911. GLHYDRLASE11.
SMARTiView protein in SMART
SM00637. CBD_II. 1 hit.
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiView protein in PROSITE
PS51173. CBM2. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.

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.
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.

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.
InterProiView protein in InterPro
IPR008965. 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.
PfamiView protein in Pfam
PF00457. Glyco_hydro_11. 1 hit.
PRINTSiPR00911. GLHYDRLASE11.
SMARTiView protein in SMART
SM00637. CBD_II. 1 hit.
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiView protein in PROSITE
PS51173. CBM2. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ56265_THEFU
AccessioniPrimary (citable) accession number: Q56265
Entry historyiIntegrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: February 15, 2017
This is version 99 of the entry and version 1 of the sequence. See 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.