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P36913 (EBA3_ELIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-beta-N-acetylglucosaminidase F3

EC=3.2.1.96
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3
Endoglycosidase F3
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3
Gene names
Name:endOF3
OrganismElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Hydrolyzes bi- and triantennary glycans. The presence of a core-bound fucose greatly augments endo F3 activity on biantennary and, presumably, triantennary oligosaccharides.

Catalytic activity

Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

Subunit structure

Monomer.

Subcellular location

Secreted.

Post-translational modification

Carbohydrate at Thr-88 consists of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939Or 40, or 41
Chain40 – 329290Endo-beta-N-acetylglucosaminidase F3
PRO_0000011957

Sites

Active site1671Proton donor By similarity

Amino acid modifications

Glycosylation881O-linked (Man...) Ref.2

Secondary structure

........................................................ 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36913 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C12EA4C8920784FF

FASTA32935,844
        10         20         30         40         50         60 
MKKIFFAQCS ILLLMLGSCS KMTEDMTPES VNKEASVKSA TALAGSNGVC IAYYITDGRN 

        70         80         90        100        110        120 
PTFKLKDIPD KVDMVILFGL KYWSLQDTTK LPGGTGMMGS FKSYKDLDTQ IRSLQSRGIK 

       130        140        150        160        170        180 
VLQNIDDDVS WQSSKPGGFA SAAAYGDAIK SIVIDKWKLD GISLDIEHSG AKPNPIPTFP 

       190        200        210        220        230        240 
GYAATGYNGW YSGSMAATPA FLNVISELTK YFGTTAPNNK QLQIASGIDV YAWNKIMENF 

       250        260        270        280        290        300 
RNNFNYIQLQ SYGANVSRTQ LMMNYATGTN KIPASKMVFG AYAEGGTNQA NDVEVAKWTP 

       310        320 
TQGAKGGMMI YTYNSNVSYA NAVRDAVKN 

« Hide

References

[1]"Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression."
Tarentino A.L., Quinones G., Changchien L.-M., Plummer T.H. Jr.
J. Biol. Chem. 268:9702-9708(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites."
Plummer T.H. Jr., Tarentino A.L., Hauer C.R.
J. Biol. Chem. 270:13192-13196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-88, IDENTIFICATION BY MASS SPECTROMETRY.
[3]"Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum."
Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N.
J. Biol. Chem. 270:13197-13203(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06332 Genomic DNA. Translation: AAA24924.1.
PIRB46678.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EOKX-ray1.80A40-329[»]
1EOMX-ray2.10A40-329[»]
ProteinModelPortalP36913.
SMRP36913. Positions 47-329.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP36913.

Entry information

Entry nameEBA3_ELIME
AccessionPrimary (citable) accession number: P36913
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries