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P36912

- EBA2_ELIME

UniProt

P36912 - EBA2_ELIME

Protein

Endo-beta-N-acetylglucosaminidase F2

Gene

endOF2

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Complex biantennary glycans are the preferred substrates. Tri- and tetraantennary glycans are not hydrolyzed, and high mannose glycans are very poor substrates.

    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 sitei171 – 1711Proton donorPROSITE-ProRule annotation

    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 F2 (EC:3.2.1.96)
    Alternative name(s):
    Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
    Endoglycosidase F2
    Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2
    Gene namesi
    Name:endOF2
    OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
    Taxonomic identifieri238 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4545Add
    BLAST
    Chaini46 – 335290Endo-beta-N-acetylglucosaminidase F2PRO_0000011956Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi73 – 731O-linked (Man...)1 Publication
    Glycosylationi89 – 891O-linked (Man...)1 Publication
    Glycosylationi143 – 1431O-linked (Man...)1 Publication

    Post-translational modificationi

    Carbohydrates at Ser-73, Ser-89 and Ser-143 consist of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP36912.
    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.
    InterProiIPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    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.

    P36912-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTANFSFAL CLSVVIMLFI KCTRSEQDLS VTKDAIAQKS GVTVSAVNLS    50
    NLIAYKNSDH QISAGYYRTW RDSATASGNL PSMRWLPDSL DMVMVFPDYT 100
    PPENAYWNTL KTNYVPYLHK RGTKVIITLG DLNSATTTGG QDSIGYSSWA 150
    KGIYDKWVGE YNLDGIDIDI ESSPSGATLT KFVAATKALS KYFGPKSGTG 200
    KTFVYDTNQN PTNFFIQTAP RYNYVFLQAY GRSTTNLTTV SGLYAPYISM 250
    KQFLPGFSFY EENGYPGNYW NDVRYPQNGT GRAYDYARWQ PATGKKGGVF 300
    SYAIERDAPL TSSNDNTLRA PNFRVTKDLI KIMNP 335
    Length:335
    Mass (Da):37,356
    Last modified:June 1, 1994 - v1
    Checksum:iFBAD1228C75F1CAF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06331 Genomic DNA. Translation: AAA24923.1.
    PIRiA46678.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06331 Genomic DNA. Translation: AAA24923.1 .
    PIRi A46678.

    3D structure databases

    ProteinModelPortali P36912.
    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 IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS01095. CHITINASE_18. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression."
      Tarentino A.L., Quinones G., Changchien L.-M., Plummer T.H. Jr.
      J. Biol. Chem. 268:9702-9708(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites."
      Plummer T.H. Jr., Tarentino A.L., Hauer C.R.
      J. Biol. Chem. 270:13192-13196(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-73; SER-89 AND SER-143, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum."
      Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N.
      J. Biol. Chem. 270:13197-13203(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiEBA2_ELIME
    AccessioniPrimary (citable) accession number: P36912
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 81 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

    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