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Reviewed, UniProtKB/Swiss-Prot P36912 (EBA2_FLAME)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

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: 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
P36912-1 [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: 8486657] [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: 7768916] [Abstract]
Cited for: GLYCOSYLATION AT SER-73; SER-89 AND SER-143, 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: 7768917] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.

Cross-references

Sequence databases

L06331 Genomic DNA. Translation: AAA24923.1.
PIRA46678.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA3.2.1.96. 39124.

Family and domain databases

InterProIPR001579. Glyco_hydro_18_chit_AS.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEBA2_FLAME
AccessionPrimary (citable) accession number: P36912
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents