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P36912 (EBA2_ELIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 F2

EC=3.2.1.96
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
Endoglycosidase F2
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2
Gene names
Name:endOF2
OrganismElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length335 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. Complex biantennary glycans are the preferred substrates. Tri- and tetraantennary glycans are not hydrolyzed, and high mannose glycans are very poor substrates.

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

Carbohydrates at Ser-73, Ser-89 and Ser-143 consist 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 termDirect 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 – 4545
Chain46 – 335290Endo-beta-N-acetylglucosaminidase F2
PRO_0000011956

Sites

Active site1711Proton donor By similarity

Amino acid modifications

Glycosylation731O-linked (Man...) Ref.2
Glycosylation891O-linked (Man...) Ref.2
Glycosylation1431O-linked (Man...) Ref.2

Sequences

Sequence LengthMass (Da)Tools
P36912 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: FBAD1228C75F1CAF

FASTA33537,356
        10         20         30         40         50         60 
MKTANFSFAL CLSVVIMLFI KCTRSEQDLS VTKDAIAQKS GVTVSAVNLS NLIAYKNSDH 

        70         80         90        100        110        120 
QISAGYYRTW RDSATASGNL PSMRWLPDSL DMVMVFPDYT PPENAYWNTL KTNYVPYLHK 

       130        140        150        160        170        180 
RGTKVIITLG DLNSATTTGG QDSIGYSSWA KGIYDKWVGE YNLDGIDIDI ESSPSGATLT 

       190        200        210        220        230        240 
KFVAATKALS KYFGPKSGTG KTFVYDTNQN PTNFFIQTAP RYNYVFLQAY GRSTTNLTTV 

       250        260        270        280        290        300 
SGLYAPYISM KQFLPGFSFY EENGYPGNYW NDVRYPQNGT GRAYDYARWQ PATGKKGGVF 

       310        320        330 
SYAIERDAPL TSSNDNTLRA PNFRVTKDLI KIMNP 

« 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 SER-73; SER-89 AND SER-143, 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 CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06331 Genomic DNA. Translation: AAA24923.1.
PIRA46678.

3D structure databases

ProteinModelPortalP36912.
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.
InterProIPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEBA2_ELIME
AccessionPrimary (citable) accession number: P36912
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 80 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries