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Protein

Endo-beta-N-acetylglucosaminidase F3

Gene

endOF3

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Hydrolyzes bi- and triantennary glycans. The presence of a core-bound fucose greatly augments endo F3 activity on biantennary and, presumably, triantennary oligosaccharides.

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)DescriptionActionsGraphical viewLength
Active sitei167Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase

Protein family/group databases

CAZyiGH18 Glycoside Hydrolase Family 18

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-N-acetylglucosaminidase F3 (EC:3.2.1.96)
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3
Endoglycosidase F3
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3
Gene namesi
Name:endOF3
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Or 40, or 41Add BLAST39
ChainiPRO_000001195740 – 329Endo-beta-N-acetylglucosaminidase F3Add BLAST290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi88O-linked (Man...) threonine1 Publication1

Post-translational modificationi

Carbohydrate at Thr-88 consists of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP36913

PTM databases

iPTMnetiP36913

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP36913
SMRiP36913
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36913

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR001223 Glyco_hydro18_cat
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00704 Glyco_hydro_18, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit

Sequencei

Sequence statusi: Complete.

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

P36913-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKIFFAQCS ILLLMLGSCS KMTEDMTPES VNKEASVKSA TALAGSNGVC
60 70 80 90 100
IAYYITDGRN PTFKLKDIPD KVDMVILFGL KYWSLQDTTK LPGGTGMMGS
110 120 130 140 150
FKSYKDLDTQ IRSLQSRGIK VLQNIDDDVS WQSSKPGGFA SAAAYGDAIK
160 170 180 190 200
SIVIDKWKLD GISLDIEHSG AKPNPIPTFP GYAATGYNGW YSGSMAATPA
210 220 230 240 250
FLNVISELTK YFGTTAPNNK QLQIASGIDV YAWNKIMENF RNNFNYIQLQ
260 270 280 290 300
SYGANVSRTQ LMMNYATGTN KIPASKMVFG AYAEGGTNQA NDVEVAKWTP
310 320
TQGAKGGMMI YTYNSNVSYA NAVRDAVKN
Length:329
Mass (Da):35,844
Last modified:June 1, 1994 - v1
Checksum:iC12EA4C8920784FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06332 Genomic DNA Translation: AAA24924.1
PIRiB46678

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06332 Genomic DNA Translation: AAA24924.1
PIRiB46678

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EOKX-ray1.80A40-329[»]
1EOMX-ray2.10A40-329[»]
ProteinModelPortaliP36913
SMRiP36913
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18 Glycoside Hydrolase Family 18

PTM databases

iPTMnetiP36913

Proteomic databases

PRIDEiP36913

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP36913

Family and domain databases

InterProiView protein in InterPro
IPR001223 Glyco_hydro18_cat
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00704 Glyco_hydro_18, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiEBA3_ELIME
AccessioniPrimary (citable) accession number: P36913
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 100 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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