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P80036

- EBAG_FLAST

UniProt

P80036 - EBAG_FLAST

Protein

Endo-beta-N-acetylglucosaminidase

Gene
N/A
Organism
Flavobacterium sp. (strain SK1022)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.1 Publication

    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.

    pH dependencei

    Optimum pH is 5.0-9.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei174 – 1741Important for substrate specificity
    Active sitei175 – 1751Proton 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 (EC:3.2.1.96)
    Alternative name(s):
    DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase
    Endo-Fsp
    Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase
    OrganismiFlavobacterium sp. (strain SK1022)
    Taxonomic identifieri148444 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601Y → A: Reduced catalytic activity. 1 Publication
    Mutagenesisi168 – 1681D → N: Loss of catalytic activity. 1 Publication
    Mutagenesisi169 – 1691G → L: Reduced catalytic activity. 1 Publication
    Mutagenesisi173 – 1731D → E or N: Reduced catalytic activity. 1 Publication
    Mutagenesisi174 – 1741D → E or N: Reduced catalytic activity toward hybrid type oligosaccharides. 1 Publication
    Mutagenesisi175 – 1751E → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi238 – 2381Y → A: Reduced catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 47471 PublicationAdd
    BLAST
    Chaini48 – 314267Endo-beta-N-acetylglucosaminidasePRO_0000077053Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP80036.
    SMRiP80036. Positions 52-311.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    P80036-1 [UniParc]FASTAAdd to Basket

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    MQFGIVAAIA DGGRTARAGG SVRPPRRPPA SHTAWGLPRG RPTGQPHATP    50
    TKSGPTSIAY VEVNNDQLAN VGRYQLANGA NAFDVAIIFA ANINWNGSKA 100
    VLYNNENVQA TLDDAATQIR PLQAKGIKVS LSILGNHQGA GIANFPTQAA 150
    AEDFAAQVSA TVSKYGLDGV DLDDEYSDYG TNGTPQPNQQ SIGWLISALR 200
    ADVPGKLISF YDIGPASSAL SSSSSTIGSK LDYAWNPYYG TYSAPSIPGL 250
    DKSRLSAAAV DVQNTPQSTA VSLAQRTKAD GYGVFMTYNL PDGDVSPYVS 300
    SMTKVLYGQA ATYH 314
    Length:314
    Mass (Da):32,936
    Last modified:January 15, 2008 - v2
    Checksum:i0227CD75BE4DC5BF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1941W → G AA sequence (PubMed:1935974)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB053207 Genomic DNA. Translation: BAB20938.1.
    PIRiS19538.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB053207 Genomic DNA. Translation: BAB20938.1 .
    PIRi S19538.

    3D structure databases

    ProteinModelPortali P80036.
    SMRi P80036. Positions 52-311.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Identification of amino acid residues essential for the substrate specificity of Flavobacterium sp. endo-beta-N-acetylglucosaminidase."
      Fujita K., Nakatake R., Yamabe K., Watanabe A., Asada Y., Takegawa K.
      Biosci. Biotechnol. Biochem. 65:1542-1548(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, MUTAGENESIS OF TYR-60; ASP-168; GLY-169; ASP-173; ASP-174; GLU-175 AND TYR-238.
    2. "Complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp."
      Takegawa K., Mikami B., Iwahara S., Morita Y., Yamamoto K., Tochikura T.
      Eur. J. Biochem. 202:175-180(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 48-314.

    Entry informationi

    Entry nameiEBAG_FLAST
    AccessioniPrimary (citable) accession number: P80036
    Secondary accession number(s): Q9F1K1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 64 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3