Reviewed, UniProtKB/Swiss-Prot P36911 (EBA1_FLAME)

Names and origin

Protein names

Recommended name:
    Endo-beta-N-acetylglucosaminidase F1
    EC=3.2.1.96
Alternative name(s):
    Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
    Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
    Endoglycosidase F1

Gene names

Name:

endOF1

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	339 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. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
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 – 50

50

Or 51, or 52 Ref.1

Chain

51 – 338

288

Endo-beta-N-acetylglucosaminidase F1

PRO_0000011954

Propeptide

339

1

Removed in mature form Probable

PRO_0000011955

Sites

Active site

182

1

Proton donor

Secondary structure

1

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339

Helix Strand Turn

Details...

Beta strand

61 – 67

7

Turn

68 – 70

3

Helix

73 – 78

6

Beta strand

79 – 81

3

Turn

82 – 84

3

Beta strand

91 – 102

12

Turn

103 – 106

4

Beta strand

107 – 111

5

Helix

114 – 121

8

Helix

123 – 126

4

Helix

128 – 132

5

Beta strand

136 – 142

7

Beta strand

145 – 147

3

Helix

155 – 172

18

Beta strand

176 – 180

5

Helix

199 – 212

14

Beta strand

216 – 223

8

Helix

224 – 226

3

Helix

238 – 240

3

Beta strand

243 – 247

5

Turn

256 – 258

3

Helix

264 – 266

3

Beta strand

267 – 273

7

Turn

274 – 277

4

Helix

282 – 291

10

Beta strand

295 – 299

5

Turn

306 – 311

6

Helix

312 – 324

13

Beta strand

328 – 330

3

Sequences

	Sequence		Length	Mass (Da)
	P36911-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 2EB8D798F9E8CF0A	FASTA	339	37,201
	10 20 30 40 50 60 MKKFINQFSA SLKNNILVFL AFPFVWTSCA RDNPLSSENS NISPNAAARA AVTGTTKANI 70 80 90 100 110 120 KLFSFTEVND TNPLNNLNFT LKNSGKPLVD MVVLFSANIN YDAANDKVFV SNNPNVQHLL 130 140 150 160 170 180 TNRAKYLKPL QDKGIKVILS ILGNHDRSGI ANLSTARAKA FAQELKNTCD LYNLDGVFFD 190 200 210 220 230 240 DEYSAYQTPP PSGFVTPSNN AAARLAYETK QAMPNKLVTV YVYSRTSSFP TAVDGVNAGS 250 260 270 280 290 300 YVDYAIHDYG GSYDLATNYP GLAKSGMVMS SQEFNQGRYA TAQALRNIVT KGYGGHMIFA 310 320 330 MDPNRSNFTS GQLPALKLIA KELYGDELVY SNTPYSKDW

References

[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: 1740434] [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: 7947807] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M80793 Genomic DNA. Translation: AAA24922.1.

PIR

A42259.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EBN	X-ray	2.00	A	51-339	[»]

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.
IPR001579. Glyco_hydro_18_chit_AS.
IPR016289. Glyco_hydro_18_end-b-GlcNAcase.
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]

PIRSF

PIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.

PROSITE

PS01095. CHITINASE_18. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

EBA1_FLAME

Accession

Primary (citable) accession number: P36911

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 66 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)