P23904 (GUB_PAEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Beta-glucanase EC=3.2.1.73 Alternative name(s): 1,3-1,4-beta-D-glucan 4-glucanohydrolase Endo-beta-1,3-1,4 glucanase Lichenase
Organism	Paenibacillus macerans (Bacillus macerans)
Taxonomic identifier	44252 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	237 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)

Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Miscellaneous	Beta-glucanases of Bacillus have a substrate range similar to lichenase of germinating barley.
Sequence similarities	Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	licheninase 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 – 23

23

Potential

Chain

24 – 237

214

Beta-glucanase

PRO_0000011789

Sites

Active site

128

1

Nucleophile By similarity

Active site

132

1

Proton donor By similarity

Amino acid modifications

Disulfide bond

55 ↔ 84

Ref.4

Experimental info

Mutagenesis

128

1

E → D, N, A, L, P, R, H, C, S or Y: Loss of activity. Ref.3

Secondary structure

1

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237

Helix Strand Turn

Details...

Beta strand

27 – 31

5

Beta strand

40 – 43

4

Beta strand

46 – 48

3

Beta strand

55 – 57

3

Helix

59 – 61

3

Beta strand

62 – 64

3

Beta strand

70 – 78

9

Beta strand

81 – 91

11

Beta strand

95 – 103

9

Beta strand

110 – 118

9

Helix

120 – 122

3

Beta strand

127 – 134

8

Helix

135 – 137

3

Beta strand

140 – 147

8

Beta strand

155 – 158

4

Helix

163 – 165

3

Beta strand

168 – 175

8

Beta strand

178 – 183

6

Beta strand

186 – 191

6

Beta strand

200 – 211

12

Helix

213 – 216

4

Beta strand

225 – 236

12

Sequences

	Sequence		Length	Mass (Da)
	P23904 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 436EABCDFFC87781	FASTA	237	26,589
	10 20 30 40 50 60 MKKKSCFTLV TTFAFSLIFS VSALAGSVFW EPLSYFNRST WEKADGYSNG GVFNCTWRAN 70 80 90 100 110 120 NVNFTNDGKL KLGLTSSAYN KFDCAEYRST NIYGYGLYEV SMKPAKNTGI VSSFFTYTGP 130 140 150 160 170 180 AHGTQWDEID IEFLGKDTTK VQFNYYTNGV GGHEKVISLG FDASKGFHTY AFDWQPGYIK 190 200 210 220 230 WYVDGVLKHT ATANIPSTPG KIMMNLWNGT GVDDWLGSYN GANPLYAEYD WVKYTSN

References

[1]	"Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases." Borriss R., Buettner K., Maentsaelae P. Mol. Gen. Genet. 222:278-283(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors." Hoej P.B., Condron R., Traeger J.C., McAuliffe J.C., Stone B.A. J. Biol. Chem. 267:25059-25066(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[3]	Olsen O. Thesis (1990), University of Aarhus, Denmark Cited for: MUTAGENESIS OF GLU-128.
[4]	"Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase." Keitel T., Simon O., Borriss R., Heinemann U. Proc. Natl. Acad. Sci. U.S.A. 90:5287-5291(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M)." Hahn M., Keitel T., Heinemann U. Eur. J. Biochem. 232:849-858(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55959 Genomic DNA. Translation: CAA39426.1.

PIR

S11927.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AJK	X-ray	1.80	A/B	40-237	[»]
1AJO	X-ray	2.07	A/B	40-237	[»]
1AXK	X-ray	2.10	A/B	26-237	[»]
1BYH	X-ray	2.80	A	40-237	[»]
1CPM	X-ray	2.00	A	40-237	[»]
1CPN	X-ray	1.80	A	26-237	[»]
1GLH	X-ray	2.00	A	40-237	[»]
1MAC	X-ray	2.30	A/B	26-237	[»]
1U0A	X-ray	1.64	A/B/C/D	40-237	[»]
2AYH	X-ray	1.60	A	40-237	[»]

ProteinModelPortal

P23904.

SMR

P23904. Positions 22-237.

ModBase

Search...

Protein family/group databases

CAZy

GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008264. Beta_glucanase.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]

Pfam

PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]

PRINTS

PR00737. GLHYDRLASE16.

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23904.

Entry information

Entry name

GUB_PAEMA

Accession

Primary (citable) accession number: P23904

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program