Reviewed, UniProtKB/Swiss-Prot P36913 (EBA3_FLAME)

Names and origin

Protein names

Recommended name:
    Endo-beta-N-acetylglucosaminidase F3
    EC=3.2.1.96
Alternative name(s):
    Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3
    Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3
    Endoglycosidase F3

Gene names

Name:

endOF3

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 activity	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.
Subunit structure	Monomer.
Subcellular location	Secreted.
Post-translational modification	Carbohydrate at Thr-88 consists of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 39

39

Or 40, or 41

Chain

40 – 329

290

Endo-beta-N-acetylglucosaminidase F3

PRO_0000011957

Sites

Active site

167

1

Proton donor By similarity

Amino acid modifications

Glycosylation

88

1

O-linked (Man...) Ref.2

Secondary structure

1

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329

Helix Strand Turn

Details...

Beta strand

49 – 55

7

Helix

65 – 67

3

Beta strand

74 – 80

7

Helix

82 – 86

5

Helix

96 – 98

3

Helix

104 – 115

12

Turn

116 – 118

3

Beta strand

120 – 126

7

Helix

129 – 132

4

Beta strand

133 – 135

3

Helix

136 – 138

3

Beta strand

139 – 141

3

Helix

142 – 153

12

Turn

154 – 157

4

Beta strand

161 – 165

5

Helix

182 – 185

4

Helix

199 – 208

10

Turn

209 – 211

3

Beta strand

216 – 218

3

Beta strand

221 – 226

6

Helix

233 – 240

8

Turn

241 – 243

3

Beta strand

245 – 249

5

Helix

256 – 268

13

Helix

274 – 276

3

Beta strand

277 – 281

5

Turn

283 – 285

3

Helix

289 – 297

9

Beta strand

307 – 310

4

Helix

313 – 315

3

Helix

317 – 327

11

Sequences

	Sequence		Length	Mass (Da)
	P36913-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: C12EA4C8920784FF	FASTA	329	35,844
	10 20 30 40 50 60 MKKIFFAQCS ILLLMLGSCS KMTEDMTPES VNKEASVKSA TALAGSNGVC IAYYITDGRN 70 80 90 100 110 120 PTFKLKDIPD KVDMVILFGL KYWSLQDTTK LPGGTGMMGS FKSYKDLDTQ IRSLQSRGIK 130 140 150 160 170 180 VLQNIDDDVS WQSSKPGGFA SAAAYGDAIK SIVIDKWKLD GISLDIEHSG AKPNPIPTFP 190 200 210 220 230 240 GYAATGYNGW YSGSMAATPA FLNVISELTK YFGTTAPNNK QLQIASGIDV YAWNKIMENF 250 260 270 280 290 300 RNNFNYIQLQ SYGANVSRTQ LMMNYATGTN KIPASKMVFG AYAEGGTNQA NDVEVAKWTP 310 320 TQGAKGGMMI YTYNSNVSYA NAVRDAVKN

References

[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: 8486657] [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: 7768916] [Abstract] Cited for: GLYCOSYLATION AT THR-88, 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: 7768917] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06332 Genomic DNA. Translation: AAA24924.1.

PIR

B46678.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EOK	X-ray	1.80	A	40-329	[»]
1EOM	X-ray	2.10	A	40-329	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA

3.2.1.96. 39124.

Family and domain databases

InterPro

IPR001223. Glyco_hydro18cat.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

PROSITE

PS01095. CHITINASE_18. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

EBA3_FLAME

Accession

Primary (citable) accession number: P36913

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 24, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)