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Q7SIE3

- Q7SIE3_BACAG

UniProt

Q7SIE3 - Q7SIE3_BACAG

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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Bacillus agaradhaerens (Bacillus agaradherans)
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941NucleophileImported
Active sitei184 – 1841Proton donor/acceptorImported

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
OrganismiBacillus agaradhaerens (Bacillus agaradherans)Imported
Taxonomic identifieri76935 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid

Keywords - PTMi

Pyrrolidone carboxylic acidImported

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7SIE3.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SIE3-1 [UniParc]FASTAAdd to Basket

« Hide

QIVTDNSIGN HDGYDYEFWK DSGGSGTMIL NHGGTFSAQW NNVNNILFRK    50
GKKFNETQTH QQVGNMSINY GANFQPNGNA YLCVYGWTVD PLVEYYIVDS 100
WGNWRPPGAT PKGTITVDGG TYDIYETLRV NQPSIKGIAT FKQYWSVRRS 150
KRTSGTISVS NHFRAWENLG MNMGKMYEVA LTVEGYQSSG SANVYSNTLR 200
INGNPLS 207
Length:207
Mass (Da):23,152
Last modified:December 15, 2003 - v1
Checksum:iC498EF0D0A085D0B
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H4G X-ray 1.10 A/B 2-207 [» ]
1QH6 X-ray 2.00 A/B 1-207 [» ]
1QH7 X-ray 1.78 A/B 1-207 [» ]
2F6B X-ray 2.80 A/B 2-206 [» ]
2NQY X-ray 2.40 A/B 2-206 [» ]
ProteinModelPortali Q7SIE3.
SMRi Q7SIE3. Positions 1-207.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Miscellaneous databases

EvolutionaryTracei Q7SIE3.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase."
    Sabini E., Sulzenbacher G., Dauter M., Dauter Z., Jorgensen P.L., Schulein M., Dupont C., Davies G.J., Wilson K.S.
    Chem. Biol. 6:483-492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-207, ACTIVE SITE, AND CARBOXYLATION AT GLN-1.
  2. "Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10)."
    Balakrishnan H., Satyanarayana L., Gaikward S., Suresh C.G.
    Submitted (NOV-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-206.
  3. "Crystal structure of alkaline thermophlic xylanase from Bacillus sp. (NCL 86-6-10) with complex xylotriose: Xylotriose cleaved to xylobiose and xylose."
    Satyanarayana L., Gaikwad S.M., Balakrishnan H., Suresh C.G.
    Submitted (NOV-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-206.

Entry informationi

Entry nameiQ7SIE3_BACAG
AccessioniPrimary (citable) accession number: Q7SIE3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: September 3, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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