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P04067

- EBAG_STRPL

UniProt

P04067 - EBAG_STRPL

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Nov 1986)
      Previous versions | rss
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    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

    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

    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 – 587
    Turni59 – 613
    Helixi64 – 696
    Beta strandi70 – 723
    Turni73 – 753
    Beta strandi77 – 793
    Beta strandi81 – 9313
    Turni94 – 974
    Beta strandi98 – 1025
    Helixi105 – 1128
    Helixi114 – 1174
    Helixi119 – 1235
    Beta strandi127 – 1348
    Beta strandi136 – 1383
    Helixi147 – 16418
    Beta strandi168 – 1725
    Helixi180 – 1823
    Helixi190 – 20112
    Beta strandi205 – 2117
    Helixi213 – 2164
    Helixi227 – 2293
    Beta strandi231 – 2344
    Beta strandi246 – 2483
    Helixi250 – 2523
    Beta strandi256 – 2594
    Turni260 – 2623
    Helixi265 – 27713
    Beta strandi282 – 2865
    Helixi294 – 30512
    Beta strandi309 – 3113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MFTPVRRRVR TAALALSAAA ALVLGSTAAS GASATPSPAP APAPAPVKQG    50
    PTSVAYVEVN NNSMLNVGKY TLADGGGNAF DVAVIFAANI NYDTGTKTAY 100
    LHFNENVQRV LDNAVTQIRP LQQQGIKVLL SVLGNHQGAG FANFPSQQAA 150
    SAFAKQLSDA VAKYGLDGVD FDDEYAEYGN NGTAQPNDSS FVHLVTALRA 200
    NMPDKIISLY NIGPAASRLS YGGVDVSDKF DYAWNPYYGT WQVPGIALPK 250
    AQLSPAAVEI GRTSRSTVAD LARRTVDEGY GVYLTYNLDG GDRTADVSAF 300
    TRELYGSEAV RTP 313
    Length:313
    Mass (Da):33,052
    Last modified:November 1, 1986 - v1
    Checksum:i69E25DE1A615CF71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02182 Genomic DNA. Translation: AAA26738.1.
    PIRiA00903. RBSMHP.

    Cross-referencesi

    Web resourcesi

    ProZyme technical fact sheet

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02182 Genomic DNA. Translation: AAA26738.1 .
    PIRi A00903. RBSMHP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 91 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