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Protein

Endo-1,4-beta-xylanase

Gene

xynJ

Organism
Bacillus sp. 41M-1
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.UniRule 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi240 – 2401Calcium 1Combined sources
Metal bindingi242 – 2421Calcium 1Combined sources
Metal bindingi259 – 2591Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi264 – 2641Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi340 – 3401Calcium 2Combined sources
Metal bindingi344 – 3441Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi345 – 3451Calcium 2Combined sources
Metal bindingi349 – 3491Calcium 1Combined sources

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

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi3.2.1.8. 11174.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11J_BACSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xynJImported
OrganismiBacillus sp. 41M-1Imported
Taxonomic identifieri98930 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 354327Endo-1,4-beta-xylanaseSequence analysisPRO_5004332952Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DCJX-ray2.24A/B1-354[»]
2DCKX-ray2.10A1-354[»]
ProteinModelPortaliQ9RC94.
SMRiQ9RC94. Positions 28-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RC94.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 223196GH11 (glycosyl hydrolase family 11)InterPro annotationAdd
BLAST
Domaini237 – 354118CBM6 (carbohydrate binding type-6)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 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.

Q9RC94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQVKIMFLM TMFLGIGLLF FSENAEAAIT SNEIGTHDGY DYEFWKDSGG
60 70 80 90 100
SGSMTLNSGG TFSAQWSNVN NILFRKGKKF DETQTHQQIG NMSINYGATY
110 120 130 140 150
NPNGNSYLTV YGWTVDPLVE FYIVDSWGTW RPPGGTPKGT INVDGGTYQI
160 170 180 190 200
YETTRYNQPS IKGTATFQQY WSVRTSKRTS GTISVSEHFR AWESLGMNMG
210 220 230 240 250
NMYEVALTVE GYQSSGSANV YSNTLTIGGQ SGGEQATRVE AESMTKGGPY
260 270 280 290 300
TSNITSPFNG VALYANGDNV SFNHSFTKAN SSFSLRGASN NSNMARVDLR
310 320 330 340 350
IGGQNRGTFY FGDQYPAVYT INNINHGIGN QLVELIVTAD DGTWDAYLDY

LEIR
Length:354
Mass (Da):39,000
Last modified:May 1, 2000 - v1
Checksum:i5F81EBB473151DC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029319 Genomic DNA. Translation: BAA82316.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029319 Genomic DNA. Translation: BAA82316.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DCJX-ray2.24A/B1-354[»]
2DCKX-ray2.10A1-354[»]
ProteinModelPortaliQ9RC94.
SMRiQ9RC94. Positions 28-353.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11J_BACSP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 11174.

Miscellaneous databases

EvolutionaryTraceiQ9RC94.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence and mutational analysis of the gene encoding the novel alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1."
    Nakai R., Wakabayashi K., Asano T., Aono R., Horikoshi K., Nakamura S.
    Nucleic Acids Symp. Ser. 31:235-236(1994)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 41M-1Imported.
  2. Kusuda J.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 41M-1Imported.
  3. "A two-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1."
    Ihsanawati, Tanaka N., Nakamura S., Kumasaka T.
    Submitted (JAN-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CALCIUM, X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiQ9RC94_9BACI
AccessioniPrimary (citable) accession number: Q9RC94
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.