Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-1,4-beta-xylanase B

Gene

xlnB

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.

Catalytic activityi

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

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei128NucleophilePROSITE-ProRule annotation1
Active sitei218Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_STRLI.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene namesi
Name:xlnB
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 411 PublicationAdd BLAST41
ChainiPRO_000000801042 – 335Endo-1,4-beta-xylanase BAdd BLAST294

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 53Combined sources7
Beta strandi56 – 64Combined sources9
Beta strandi67 – 72Combined sources6
Beta strandi77 – 84Combined sources8
Beta strandi86 – 96Combined sources11
Beta strandi101 – 123Combined sources23
Turni124 – 126Combined sources3
Beta strandi127 – 137Combined sources11
Beta strandi143 – 150Combined sources8
Beta strandi153 – 165Combined sources13
Beta strandi170 – 183Combined sources14
Beta strandi187 – 191Combined sources5
Helixi192 – 201Combined sources10
Beta strandi213 – 231Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EJ3X-ray1.31A/B1-234[»]
ProteinModelPortaliP26515.
SMRiP26515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 230GH11PROSITE-ProRule annotationAdd BLAST187
Domaini243 – 335CBM2PROSITE-ProRule annotationAdd BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 249Linker ("hinge") (Gly-rich box)Add BLAST19

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation
Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLVQPRRR RRGPVTLLVR SAWAVALAAL AALMLPGTAQ ADTVVTTNQE
60 70 80 90 100
GTNNGYYYSF WTDSQGTVSM NMGSGGQYST SWRNTGNFVA GKGWANGGRR
110 120 130 140 150
TVQYSGSFNP SGNAYLALYG WTSNPLVEYY IVDNWGTYRP TGEYKGTVTS
160 170 180 190 200
DGGTYDIYKT TRVNKPSVEG TRTFDQYWSV RQSKRTGGTI TTGNHFDAWA
210 220 230 240 250
RAGMPLGNFS YYMIMATEGY QSSGSSSINV GGTGGGDSGG GDNGGGGGGC
260 270 280 290 300
TATVSAGQKW GDRYNLDVSV SGASDWTVTM NVPSPAKVLS NWNVNASYPS
310 320 330
AQTLTARLNG SGNNWGATIQ ANANWTWPSV SCSAG
Length:335
Mass (Da):35,575
Last modified:August 14, 2001 - v3
Checksum:i513B1458BF8FF0CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64552 Genomic DNA. Translation: AAC06114.2.
PIRiJS0590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64552 Genomic DNA. Translation: AAC06114.2.
PIRiJS0590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EJ3X-ray1.31A/B1-234[»]
ProteinModelPortaliP26515.
SMRiP26515.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_STRLI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

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...

Entry informationi

Entry nameiXYNB_STRLI
AccessioniPrimary (citable) accession number: P26515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 14, 2001
Last modified: November 30, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

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.