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Protein

Endo-1,4-beta-xylanase

Gene

xynA

Organism
Bacillus subtilis
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 annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotationImported

Enzyme and pathway databases

UniPathwayiUPA00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xynAImported
OrganismiBacillus subtilisImported
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 213185Endo-1,4-beta-xylanaseSequence analysisPRO_5004252328Add
BLAST

Proteomic databases

PaxDbiQ59254.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010386.

Structurei

3D structure databases

ProteinModelPortaliQ59254.
SMRiQ59254. Positions 29-213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 213194GH11 (glycosyl hydrolase family 11)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.
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.

Q59254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKFKKNFLV GLSAALMSIS LFPATASAAS 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 TITFSNHVNA WKSHGMNLGS NWAYQVMATE
210
GYQSSGSSNV TVW
Length:213
Mass (Da):23,355
Last modified:November 1, 1996 - v1
Checksum:i21D76D4FE8CED4B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34519 Genomic DNA. Translation: CAA84276.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34519 Genomic DNA. Translation: CAA84276.1.

3D structure databases

ProteinModelPortaliQ59254.
SMRiQ59254. Positions 29-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010386.

Proteomic databases

PaxDbiQ59254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
ENOG410YH6C. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.

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...

Publicationsi

  1. "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase."
    Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J.
    Mol. Gen. Genet. 231:332-336(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 168 trpC2Imported.
  2. "Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus subtilis: characterization, mapping and construction of strains deficient in lichenase, cellulase and xylanase."
    Wolf M., Geczi A., Simon O., Borriss R.
    Microbiology 141:281-290(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 168 trpC2Imported.
  3. Borriss R., Wolf M.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 168 trpC2Imported.

Entry informationi

Entry nameiQ59254_BACIU
AccessioniPrimary (citable) accession number: Q59254
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 75 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.