Reviewed, UniProtKB/Swiss-Prot P04067 (EBAG_STRPL)

Names and origin

Protein names	Recommended name:     Endo-beta-N-acetylglucosaminidase H     EC=3.2.1.96 Alternative name(s):     Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase H     DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase H     Endoglycosidase H       Short name=Endo H
Organism	Streptomyces plicatus
Taxonomic identifier	1922 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	313 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	Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
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: InterPro
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 – 41

41

Or 43

Chain

42 – 313

272

Endo-beta-N-acetylglucosaminidase H

PRO_0000011958

Sites

Active site

174

1

Proton donor

Secondary structure

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313

Helix Strand Turn

Details...

Beta strand

50 – 58

9

Turn

59 – 61

3

Helix

64 – 69

6

Beta strand

70 – 72

3

Turn

73 – 76

4

Beta strand

77 – 79

3

Beta strand

81 – 93

13

Turn

94 – 97

4

Beta strand

98 – 102

5

Helix

105 – 112

8

Helix

114 – 117

4

Helix

119 – 123

5

Beta strand

127 – 134

8

Beta strand

136 – 138

3

Helix

147 – 163

17

Beta strand

168 – 172

5

Helix

180 – 182

3

Helix

190 – 201

12

Beta strand

205 – 211

7

Helix

214 – 217

4

Helix

227 – 229

3

Beta strand

231 – 234

4

Beta strand

246 – 248

3

Helix

250 – 252

3

Beta strand

256 – 259

4

Turn

260 – 262

3

Helix

265 – 277

13

Beta strand

282 – 286

5

Helix

294 – 304

11

Beta strand

309 – 311

3

Sequences

	Sequence		Length	Mass (Da)
	P04067-1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 69E25DE1A615CF71	FASTA	313	33,052
	10 20 30 40 50 60 MFTPVRRRVR TAALALSAAA ALVLGSTAAS GASATPSPAP APAPAPVKQG PTSVAYVEVN 70 80 90 100 110 120 NNSMLNVGKY TLADGGGNAF DVAVIFAANI NYDTGTKTAY LHFNENVQRV LDNAVTQIRP 130 140 150 160 170 180 LQQQGIKVLL SVLGNHQGAG FANFPSQQAA SAFAKQLSDA VAKYGLDGVD FDDEYAEYGN 190 200 210 220 230 240 NGTAQPNDSS FVHLVTALRA NMPDKIISLY NIGPAASRLS YGGVDVSDKF DYAWNPYYGT 250 260 270 280 290 300 WQVPGIALPK AQLSPAAVEI GRTSRSTVAD LARRTVDEGY GVYLTYNLDG GDRTADVSAF 310 TRELYGSEAV RTP

References

[1]	"Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H." Robbins P.W., Trimble R.B., Wirth D.F., Hering C., Maley F., Maley G.F., Das R., Gibson B.W., Royal N., Biemann K. J. Biol. Chem. 259:7577-7583(1984) [PubMed: 6429133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9-A resolution: active-site geometry and substrate recognition." Rao V., Guan C., Van Roey P. Structure 3:449-457(1995) [PubMed: 7663942] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]	"Mutations of endo-beta-N-acetylglucosaminidase H active site residue Assp130 and Glu132: activities and conformations." Rao V., Cui T., Guan C., Van Roey P. Protein Sci. 8:2338-2346(1999) [PubMed: 10595536] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 48-312 OF MUTANTS.

Web resources

ProZyme technical fact sheet

Cross-references

Sequence databases

EMBLGenBankDDBJ

K02182 Genomic DNA. Translation: AAA26738.1.

PIR

RBSMHP. A00903.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C3F	X-ray	2.10	A	48-312	[»]
1C8X	X-ray	2.00	A	48-312	[»]
1C8Y	X-ray	2.00	A	48-312	[»]
1C90	X-ray	2.10	A/B	48-312	[»]
1C91	X-ray	2.10	A	48-312	[»]
1C92	X-ray	2.10	A	48-312	[»]
1C93	X-ray	2.10	A	48-312	[»]
1EDT	X-ray	1.90	A	43-313	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA

3.2.1.96. 39142.

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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

EBAG_STRPL

Accession

Primary (citable) accession number: P04067

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	June 16, 2009
This is version 72 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)