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Protein

Endo-beta-N-acetylglucosaminidase H

Gene
N/A
Organism
Streptomyces plicatus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.2 Publications

Catalytic activityi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei174Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiStreptomyces plicatus
Taxonomic identifieri1922 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172D → A or E: 2% activity. 1 Publication1
Mutagenesisi172D → N: 0.1% activity. 1 Publication1
Mutagenesisi174E → A: Loss of activity. 1 Publication1
Mutagenesisi174E → D or Q: 0.05% activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Or 441 PublicationAdd BLAST42
ChainiPRO_000001195843 – 313Endo-beta-N-acetylglucosaminidase HAdd BLAST271

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 58Combined sources7
Turni59 – 61Combined sources3
Helixi64 – 69Combined sources6
Beta strandi70 – 72Combined sources3
Turni73 – 75Combined sources3
Beta strandi77 – 79Combined sources3
Beta strandi81 – 93Combined sources13
Turni94 – 97Combined sources4
Beta strandi98 – 102Combined sources5
Helixi105 – 112Combined sources8
Helixi114 – 117Combined sources4
Helixi119 – 123Combined sources5
Beta strandi127 – 134Combined sources8
Beta strandi136 – 138Combined sources3
Helixi147 – 164Combined sources18
Beta strandi168 – 172Combined sources5
Helixi180 – 182Combined sources3
Helixi190 – 201Combined sources12
Beta strandi205 – 211Combined sources7
Helixi213 – 216Combined sources4
Helixi227 – 229Combined sources3
Beta strandi231 – 234Combined sources4
Beta strandi246 – 248Combined sources3
Helixi250 – 252Combined sources3
Beta strandi256 – 259Combined sources4
Turni260 – 262Combined sources3
Helixi265 – 277Combined sources13
Beta strandi282 – 286Combined sources5
Helixi294 – 305Combined sources12
Beta strandi309 – 311Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP04067.
SMRiP04067.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04067.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFiPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTPVRRRVR TAALALSAAA ALVLGSTAAS GASATPSPAP APAPAPVKQG
60 70 80 90 100
PTSVAYVEVN NNSMLNVGKY TLADGGGNAF DVAVIFAANI NYDTGTKTAY
110 120 130 140 150
LHFNENVQRV LDNAVTQIRP LQQQGIKVLL SVLGNHQGAG FANFPSQQAA
160 170 180 190 200
SAFAKQLSDA VAKYGLDGVD FDDEYAEYGN NGTAQPNDSS FVHLVTALRA
210 220 230 240 250
NMPDKIISLY NIGPAASRLS YGGVDVSDKF DYAWNPYYGT WQVPGIALPK
260 270 280 290 300
AQLSPAAVEI GRTSRSTVAD LARRTVDEGY GVYLTYNLDG GDRTADVSAF
310
TRELYGSEAV RTP
Length:313
Mass (Da):33,052
Last modified:November 1, 1986 - v1
Checksum:i69E25DE1A615CF71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02182 Genomic DNA. Translation: AAA26738.1.
PIRiA00903. RBSMHP.

Cross-referencesi

Web resourcesi

ProZyme product sheet

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02182 Genomic DNA. Translation: AAA26738.1.
PIRiA00903. RBSMHP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP04067.
SMRiP04067.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04067.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFiPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEBAG_STRPL
AccessioniPrimary (citable) accession number: P04067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 2, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.