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P04067 (EBAG_STRPL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=3.2.1.96
Alternative name(s):
DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase H
Endoglycosidase H
Short name=Endo H
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase H
OrganismStreptomyces plicatus
Taxonomic identifier1922 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   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: InterPro

   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 – 4141Or 43
Chain42 – 313272Endo-beta-N-acetylglucosaminidase H
PRO_0000011958

Sites

Active site1741Proton donor

Secondary structure

....................................................... 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04067 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 69E25DE1A615CF71

FASTA31333,052
        10         20         30         40         50         60 
MFTPVRRRVR TAALALSAAA ALVLGSTAAS GASATPSPAP APAPAPVKQG PTSVAYVEVN 

        70         80         90        100        110        120 
NNSMLNVGKY TLADGGGNAF DVAVIFAANI NYDTGTKTAY LHFNENVQRV LDNAVTQIRP 

       130        140        150        160        170        180 
LQQQGIKVLL SVLGNHQGAG FANFPSQQAA SAFAKQLSDA VAKYGLDGVD FDDEYAEYGN 

       190        200        210        220        230        240 
NGTAQPNDSS FVHLVTALRA NMPDKIISLY NIGPAASRLS YGGVDVSDKF DYAWNPYYGT 

       250        260        270        280        290        300 
WQVPGIALPK AQLSPAAVEI GRTSRSTVAD LARRTVDEGY GVYLTYNLDG GDRTADVSAF 

       310 
TRELYGSEAV RTP 

« Hide

References

[1]"Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H."
Robbins P.W., Trimble R.B., Wirth D.F., Hering C., Maley F., Maley G.F., Das R., Gibson B.W., Royal N., Biemann K.
J. Biol. Chem. 259:7577-7583(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9-A resolution: active-site geometry and substrate recognition."
Rao V., Guan C., Van Roey P.
Structure 3:449-457(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]"Mutations of endo-beta-N-acetylglucosaminidase H active site residue Assp130 and Glu132: activities and conformations."
Rao V., Cui T., Guan C., Van Roey P.
Protein Sci. 8:2338-2346(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 48-312 OF MUTANTS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02182 Genomic DNA. Translation: AAA26738.1.
PIRRBSMHP. A00903.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3FX-ray2.10A48-312[»]
1C8XX-ray2.00A48-312[»]
1C8YX-ray2.00A48-312[»]
1C90X-ray2.10A/B48-312[»]
1C91X-ray2.10A48-312[»]
1C92X-ray2.10A48-312[»]
1C93X-ray2.10A48-312[»]
1EDTX-ray1.90A43-313[»]
ProteinModelPortalP04067.
SMRP04067. Positions 48-312.
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.
IPR001579. Glyco_hydro_18_chit_AS.
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.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04067.

Entry information

Entry nameEBAG_STRPL
AccessionPrimary (citable) accession number: P04067
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: October 16, 2013
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