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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Salipaludibacillus agaradhaerens (Bacillus agaradhaerens)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 sitei94NucleophilePROSITE-ProRule annotationCombined sources1
Active sitei184Proton donorPROSITE-ProRule annotation1
Active sitei184Proton donor/acceptorCombined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidasePROSITE-ProRule annotation, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradationPROSITE-ProRule annotation

Enzyme and pathway databases

UniPathwayiUPA00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanasePROSITE-ProRule annotation (EC:3.2.1.8PROSITE-ProRule annotation)
OrganismiSalipaludibacillus agaradhaerens (Bacillus agaradhaerens)Imported
Taxonomic identifieri76935 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceae

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acidCombined sources1

Keywords - PTMi

Pyrrolidone carboxylic acidCombined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H4GX-ray1.10A/B1-207[»]
1QH6X-ray2.00A/B1-207[»]
1QH7X-ray1.78A/B1-207[»]
2F6BX-ray2.80A/B2-206[»]
2NQYX-ray2.40A/B1-206[»]
ProteinModelPortaliQ7SIE3.
SMRiQ7SIE3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIE3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 197GH11InterPro annotationAdd BLAST196

Sequence similaritiesi

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

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiView protein in InterPro
IPR013320. ConA-like_dom_sf.
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.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiView protein in PROSITE
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7SIE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QIVTDNSIGN HDGYDYEFWK DSGGSGTMIL NHGGTFSAQW NNVNNILFRK
60 70 80 90 100
GKKFNETQTH QQVGNMSINY GANFQPNGNA YLCVYGWTVD PLVEYYIVDS
110 120 130 140 150
WGNWRPPGAT PKGTITVDGG TYDIYETLRV NQPSIKGIAT FKQYWSVRRS
160 170 180 190 200
KRTSGTISVS NHFRAWENLG MNMGKMYEVA LTVEGYQSSG SANVYSNTLR

INGNPLS
Length:207
Mass (Da):23,152
Last modified:December 15, 2003 - v1
Checksum:iC498EF0D0A085D0B
GO

Similar proteinsi

Entry informationi

Entry nameiQ7SIE3_SALAG
AccessioniPrimary (citable) accession number: Q7SIE3
Entry historyiIntegrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: November 22, 2017
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources