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P36911 (EBA1_ELIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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 F1

EC=3.2.1.96
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
Endoglycosidase F1
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
Gene names
Name:endOF1
OrganismElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length339 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. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   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 – 5050Or 51, or 52 Ref.1
Chain51 – 338288Endo-beta-N-acetylglucosaminidase F1
PRO_0000011954
Propeptide3391Removed in mature form Probable
PRO_0000011955

Sites

Active site1821Proton donor

Secondary structure

.................................................. 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36911 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 2EB8D798F9E8CF0A

FASTA33937,201
        10         20         30         40         50         60 
MKKFINQFSA SLKNNILVFL AFPFVWTSCA RDNPLSSENS NISPNAAARA AVTGTTKANI 

        70         80         90        100        110        120 
KLFSFTEVND TNPLNNLNFT LKNSGKPLVD MVVLFSANIN YDAANDKVFV SNNPNVQHLL 

       130        140        150        160        170        180 
TNRAKYLKPL QDKGIKVILS ILGNHDRSGI ANLSTARAKA FAQELKNTCD LYNLDGVFFD 

       190        200        210        220        230        240 
DEYSAYQTPP PSGFVTPSNN AAARLAYETK QAMPNKLVTV YVYSRTSSFP TAVDGVNAGS 

       250        260        270        280        290        300 
YVDYAIHDYG GSYDLATNYP GLAKSGMVMS SQEFNQGRYA TAQALRNIVT KGYGGHMIFA 

       310        320        330 
MDPNRSNFTS GQLPALKLIA KELYGDELVY SNTPYSKDW 

« Hide

References

[1]"Multiple endoglycosidase (Endo) F activities expressed by Flavobacterium meningosepticum. Endo F1: molecular cloning, primary sequence, and structural relationship to Endo H."
Tarentino A.L., Quinones G., Schrader W.P., Changchien L.-M., Plummer T.H. Jr.
J. Biol. Chem. 267:3868-3872(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 51-77; 108-161 AND 265-338.
[2]"Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate."
van Roey P., Rao V., Plummer T.H. Jr., Tarentino A.L.
Biochemistry 33:13989-13996(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80793 Genomic DNA. Translation: AAA24922.1.
PIRA42259.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBNX-ray2.00A51-339[»]
ProteinModelPortalP36911.
SMRP36911. Positions 55-339.
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.
InterProIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP36911.

Entry information

Entry nameEBA1_ELIME
AccessionPrimary (citable) accession number: P36911
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 84 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