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Protein

Endo-beta-N-acetylglucosaminidase F3

Gene

endOF3

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, 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

Complete GO annotation...

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...)1 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

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 55Combined sources7
Helixi65 – 67Combined sources3
Beta strandi74 – 80Combined sources7
Helixi82 – 86Combined sources5
Helixi96 – 98Combined sources3
Beta strandi101 – 103Combined sources3
Helixi104 – 115Combined sources12
Turni116 – 118Combined sources3
Beta strandi120 – 126Combined sources7
Helixi129 – 132Combined sources4
Beta strandi133 – 135Combined sources3
Helixi136 – 138Combined sources3
Beta strandi139 – 141Combined sources3
Helixi142 – 153Combined sources12
Turni154 – 157Combined sources4
Beta strandi161 – 165Combined sources5
Helixi182 – 185Combined sources4
Beta strandi186 – 189Combined sources4
Helixi199 – 208Combined sources10
Turni209 – 211Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi221 – 226Combined sources6
Helixi233 – 240Combined sources8
Turni241 – 243Combined sources3
Beta strandi245 – 249Combined sources5
Helixi256 – 268Combined sources13
Helixi274 – 276Combined sources3
Beta strandi277 – 281Combined sources5
Turni283 – 285Combined sources3
Helixi289 – 297Combined sources9
Beta strandi307 – 310Combined sources4
Helixi313 – 315Combined sources3
Helixi317 – 327Combined sources11

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...

Miscellaneous databases

EvolutionaryTraceiP36913.

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.
InterProiIPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
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.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP36913.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEBA3_ELIME
AccessioniPrimary (citable) accession number: P36913
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.