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P36913

- EBA3_ELIME

UniProt

P36913 - EBA3_ELIME

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Protein
Endo-beta-N-acetylglucosaminidase F3
Gene
endOF3
Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671Proton donor By similarity

GO - Molecular functioni

  1. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Or 40, or 41
Add
BLAST
Chaini40 – 329290Endo-beta-N-acetylglucosaminidase F3
PRO_0000011957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881O-linked (Man...)1 Publication

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 557
Helixi65 – 673
Beta strandi74 – 807
Helixi82 – 865
Helixi96 – 983
Beta strandi101 – 1033
Helixi104 – 11512
Turni116 – 1183
Beta strandi120 – 1267
Helixi129 – 1324
Beta strandi133 – 1353
Helixi136 – 1383
Beta strandi139 – 1413
Helixi142 – 15312
Turni154 – 1574
Beta strandi161 – 1655
Helixi182 – 1854
Beta strandi186 – 1894
Helixi199 – 20810
Turni209 – 2113
Beta strandi216 – 2183
Beta strandi221 – 2266
Helixi233 – 2408
Turni241 – 2433
Beta strandi245 – 2495
Helixi256 – 26813
Helixi274 – 2763
Beta strandi277 – 2815
Turni283 – 2853
Helixi289 – 2979
Beta strandi307 – 3104
Helixi313 – 3153
Helixi317 – 32711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EOKX-ray1.80A40-329[»]
1EOMX-ray2.10A40-329[»]
ProteinModelPortaliP36913.
SMRiP36913. Positions 47-329.

Miscellaneous databases

EvolutionaryTraceiP36913.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18cat.
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

MKKIFFAQCS ILLLMLGSCS KMTEDMTPES VNKEASVKSA TALAGSNGVC    50
IAYYITDGRN PTFKLKDIPD KVDMVILFGL KYWSLQDTTK LPGGTGMMGS 100
FKSYKDLDTQ IRSLQSRGIK VLQNIDDDVS WQSSKPGGFA SAAAYGDAIK 150
SIVIDKWKLD GISLDIEHSG AKPNPIPTFP GYAATGYNGW YSGSMAATPA 200
FLNVISELTK YFGTTAPNNK QLQIASGIDV YAWNKIMENF RNNFNYIQLQ 250
SYGANVSRTQ LMMNYATGTN KIPASKMVFG AYAEGGTNQA NDVEVAKWTP 300
TQGAKGGMMI YTYNSNVSYA NAVRDAVKN 329
Length:329
Mass (Da):35,844
Last modified:June 1, 1994 - v1
Checksum:iC12EA4C8920784FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06332 Genomic DNA. Translation: AAA24924.1.
PIRiB46678.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06332 Genomic DNA. Translation: AAA24924.1 .
PIRi B46678.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EOK X-ray 1.80 A 40-329 [» ]
1EOM X-ray 2.10 A 40-329 [» ]
ProteinModelPortali P36913.
SMRi P36913. Positions 47-329.
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 P36913.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
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 THR-88, 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 CARBOHYDRATE, IDENTIFICATION BY MASS SPECTROMETRY.

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: April 16, 2014
This is version 89 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

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