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P04067

- EBAG_STRPL

UniProt

P04067 - EBAG_STRPL

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Protein

Endo-beta-N-acetylglucosaminidase H

Gene
N/A
Organism
Streptomyces plicatus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei174 – 1741Proton donor

GO - Molecular functioni

  1. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Or 43Add
BLAST
Chaini42 – 313272Endo-beta-N-acetylglucosaminidase HPRO_0000011958Add
BLAST

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 587Combined sources
Turni59 – 613Combined sources
Helixi64 – 696Combined sources
Beta strandi70 – 723Combined sources
Turni73 – 753Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 9313Combined sources
Turni94 – 974Combined sources
Beta strandi98 – 1025Combined sources
Helixi105 – 1128Combined sources
Helixi114 – 1174Combined sources
Helixi119 – 1235Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi136 – 1383Combined sources
Helixi147 – 16418Combined sources
Beta strandi168 – 1725Combined sources
Helixi180 – 1823Combined sources
Helixi190 – 20112Combined sources
Beta strandi205 – 2117Combined sources
Helixi213 – 2164Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi246 – 2483Combined sources
Helixi250 – 2523Combined sources
Beta strandi256 – 2594Combined sources
Turni260 – 2623Combined sources
Helixi265 – 27713Combined sources
Beta strandi282 – 2865Combined sources
Helixi294 – 30512Combined sources
Beta strandi309 – 3113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 48-312.
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_hydro18cat.
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 technical fact sheet

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02182 Genomic DNA. Translation: AAA26738.1 .
PIRi A00903. RBSMHP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C3F X-ray 2.10 A 48-312 [» ]
1C8X X-ray 2.00 A 48-312 [» ]
1C8Y X-ray 2.00 A 48-312 [» ]
1C90 X-ray 2.10 A/B 48-312 [» ]
1C91 X-ray 2.10 A 48-312 [» ]
1C92 X-ray 2.10 A 48-312 [» ]
1C93 X-ray 2.10 A 48-312 [» ]
1EDT X-ray 1.90 A 43-313 [» ]
ProteinModelPortali P04067.
SMRi P04067. Positions 48-312.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P04067.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
PIRSFi PIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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 26, 2014
This is version 92 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

External Data

Dasty 3