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P36911

- EBA1_ELIME

UniProt

P36911 - EBA1_ELIME

Protein

Endo-beta-N-acetylglucosaminidase F1

Gene

endOF1

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 85 (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. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis.

    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 sitei182 – 1821Proton 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 F1 (EC:3.2.1.96)
    Alternative name(s):
    Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
    Endoglycosidase F1
    Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
    Gene namesi
    Name:endOF1
    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 – 5050Or 51, or 521 PublicationAdd
    BLAST
    Chaini51 – 338288Endo-beta-N-acetylglucosaminidase F1PRO_0000011954Add
    BLAST
    Propeptidei339 – 3391Removed in mature formCuratedPRO_0000011955

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 677
    Turni68 – 703
    Helixi73 – 786
    Beta strandi79 – 813
    Turni82 – 843
    Beta strandi91 – 10212
    Turni103 – 1064
    Beta strandi107 – 1115
    Helixi114 – 1218
    Helixi123 – 1264
    Helixi128 – 1325
    Beta strandi136 – 1427
    Beta strandi145 – 1473
    Helixi155 – 17218
    Beta strandi176 – 1805
    Helixi199 – 21214
    Beta strandi216 – 2238
    Helixi224 – 2263
    Helixi238 – 2403
    Beta strandi243 – 2475
    Turni256 – 2583
    Helixi264 – 2663
    Beta strandi267 – 2737
    Turni274 – 2774
    Helixi282 – 29110
    Beta strandi295 – 2995
    Turni306 – 3116
    Helixi312 – 32413
    Beta strandi328 – 3303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EBNX-ray2.00A51-339[»]
    ProteinModelPortaliP36911.
    SMRiP36911. Positions 55-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36911.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    P36911-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKFINQFSA SLKNNILVFL AFPFVWTSCA RDNPLSSENS NISPNAAARA    50
    AVTGTTKANI KLFSFTEVND TNPLNNLNFT LKNSGKPLVD MVVLFSANIN 100
    YDAANDKVFV SNNPNVQHLL TNRAKYLKPL QDKGIKVILS ILGNHDRSGI 150
    ANLSTARAKA FAQELKNTCD LYNLDGVFFD DEYSAYQTPP PSGFVTPSNN 200
    AAARLAYETK QAMPNKLVTV YVYSRTSSFP TAVDGVNAGS YVDYAIHDYG 250
    GSYDLATNYP GLAKSGMVMS SQEFNQGRYA TAQALRNIVT KGYGGHMIFA 300
    MDPNRSNFTS GQLPALKLIA KELYGDELVY SNTPYSKDW 339
    Length:339
    Mass (Da):37,201
    Last modified:June 1, 1994 - v1
    Checksum:i2EB8D798F9E8CF0A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80793 Genomic DNA. Translation: AAA24922.1.
    PIRiA42259.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80793 Genomic DNA. Translation: AAA24922.1 .
    PIRi A42259.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EBN X-ray 2.00 A 51-339 [» ]
    ProteinModelPortali P36911.
    SMRi P36911. Positions 55-339.
    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 P36911.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR016289. Endo-Fsp.
    IPR001223. Glyco_hydro18cat.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Multiple endoglycosidase (Endo) F activities expressed by Flavobacterium meningosepticum. Endo F1: molecular cloning, primary sequence, and structural relationship to Endo H."
      Tarentino A.L., Quinones G., Schrader W.P., Changchien L.-M., Plummer T.H. Jr.
      J. Biol. Chem. 267:3868-3872(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 51-77; 108-161 AND 265-338.
    2. "Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate."
      van Roey P., Rao V., Plummer T.H. Jr., Tarentino A.L.
      Biochemistry 33:13989-13996(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiEBA1_ELIME
    AccessioniPrimary (citable) accession number: P36911
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 85 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