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Protein

Endo-1,4-beta-xylanase

Gene

xlnA

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 sitei106NucleophilePROSITE-ProRule annotation1 Publication1
Active sitei200Proton donorPROSITE-ProRule annotation1 Publication1

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

BRENDAi3.2.1.8. 649.
SABIO-RKP09850.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_BACCI.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Gene namesi
Name:xlnA
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000000799629 – 213Endo-1,4-beta-xylanase1 PublicationAdd BLAST185

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 38Combined sources6
Beta strandi42 – 48Combined sources7
Beta strandi53 – 60Combined sources8
Beta strandi62 – 72Combined sources11
Beta strandi78 – 101Combined sources24
Turni102 – 104Combined sources3
Beta strandi105 – 115Combined sources11
Beta strandi121 – 128Combined sources8
Beta strandi131 – 144Combined sources14
Beta strandi148 – 162Combined sources15
Beta strandi166 – 168Combined sources3
Beta strandi170 – 173Combined sources4
Helixi174 – 183Combined sources10
Beta strandi190 – 203Combined sources14
Beta strandi205 – 213Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCXX-ray1.81A29-213[»]
1BVVX-ray1.80A29-213[»]
1C5HX-ray1.55A29-213[»]
1C5IX-ray1.80A29-213[»]
1HV0X-ray1.60A29-213[»]
1HV1X-ray1.80A29-213[»]
1XNBX-ray1.49A29-213[»]
1XNCX-ray1.60A29-213[»]
2BVVX-ray1.50A29-213[»]
3LB9X-ray3.00A/B/C29-213[»]
3VZJX-ray2.41A/B/C/D29-213[»]
3VZKX-ray1.55A/B29-213[»]
3VZLX-ray2.00A/B/C/D29-213[»]
3VZMX-ray1.86A29-213[»]
3VZNX-ray1.67A/B29-213[»]
3VZOX-ray1.73A29-213[»]
ProteinModelPortaliP09850.
SMRiP09850.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09850.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 213GH11PROSITE-ProRule annotationAdd BLAST185

Sequence similaritiesi

Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. 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.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. 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.

P09850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS
60 70 80 90 100
GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT
110 120 130 140 150
RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR
160 170 180 190 200
TTFTQYWSVR QSKRPTGSNA TITFTNHVNA WKSHGMNLGS NWAYQVMATE
210
GYQSSGSSNV TVW
Length:213
Mass (Da):23,359
Last modified:July 1, 1989 - v1
Checksum:i4BA0A35238CC0135
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1.
PIRiS01734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1.
PIRiS01734.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCXX-ray1.81A29-213[»]
1BVVX-ray1.80A29-213[»]
1C5HX-ray1.55A29-213[»]
1C5IX-ray1.80A29-213[»]
1HV0X-ray1.60A29-213[»]
1HV1X-ray1.80A29-213[»]
1XNBX-ray1.49A29-213[»]
1XNCX-ray1.60A29-213[»]
2BVVX-ray1.50A29-213[»]
3LB9X-ray3.00A/B/C29-213[»]
3VZJX-ray2.41A/B/C/D29-213[»]
3VZKX-ray1.55A/B29-213[»]
3VZLX-ray2.00A/B/C/D29-213[»]
3VZMX-ray1.86A29-213[»]
3VZNX-ray1.67A/B29-213[»]
3VZOX-ray1.73A29-213[»]
ProteinModelPortaliP09850.
SMRiP09850.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_BACCI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 649.
SABIO-RKP09850.

Miscellaneous databases

EvolutionaryTraceiP09850.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. 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.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNA_BACCI
AccessioniPrimary (citable) accession number: P09850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 102 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

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.