Reviewed, UniProtKB/Swiss-Prot P12257 (GUB2_HORVU)

Names and origin

Protein names	Recommended name:     Lichenase-2     EC=3.2.1.73 Alternative name(s):     Lichenase II     Endo-beta-1,3-1,4 glucanase II     (1->3,1->4)-beta-glucanase isoenzyme EII
Organism	Hordeum vulgare (Barley)
Taxonomic identifier	4513 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	312 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues.
Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Pathway	Glycan metabolism; beta-D-glucan degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
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
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro 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 – 6

›6

Ref.2

Chain

7 – 312

306

Lichenase-2

PRO_0000011897

Sites

Active site

238

1

Nucleophile

Active site

294

1

Proton donor

Amino acid modifications

Glycosylation

196

1

N-linked (GlcNAc...)

Experimental info

Non-terminal residue

1

1

Secondary structure

1

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312

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

21 – 31

11

Beta strand

35 – 40

6

Helix

43 – 49

7

Beta strand

55 – 60

6

Helix

62 – 64

3

Helix

65 – 70

6

Helix

72 – 82

11

Turn

83 – 85

3

Beta strand

89 – 99

11

Helix

102 – 107

6

Helix

108 – 121

14

Beta strand

127 – 134

8

Helix

135 – 137

3

Beta strand

138 – 140

3

Helix

144 – 146

3

Helix

151 – 167

17

Beta strand

171 – 174

4

Helix

177 – 183

7

Helix

190 – 194

5

Beta strand

201 – 204

4

Beta strand

207 – 209

3

Helix

212 – 225

14

Turn

226 – 228

3

Beta strand

234 – 238

5

Beta strand

243 – 246

4

Helix

251 – 264

14

Turn

265 – 267

3

Beta strand

270 – 274

5

Beta strand

278 – 281

4

Helix

293 – 295

3

Beta strand

306 – 308

3

Sequences

	Sequence		Length	Mass (Da)
	P12257-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 7D18C2A6DF522E17	FASTA	312	32,774
	10 20 30 40 50 60 PPSVESIGVC YGMSANNLPA ASTVVSMFKF NGIKSMRLYA PNQAALQAVG GTGINVVVGA 70 80 90 100 110 120 PNDVLSNLAA SPAAAASWVK SNIQAYPKVS FRYVCVGNEV AGGATRNLVP AMKNVHGALV 130 140 150 160 170 180 AAGLGHIKVT TSVSQAILGV FSPPSAGSFT GEAAAFMGPV VQFLARTNAP LMANIYPYLA 190 200 210 220 230 240 WAYNPSAMDM GYALFNASGT VVRDGAYGYQ NLFDTTVDAF YTAMGKHGGS SVKLVVSESG 250 260 270 280 290 300 WPSGGGTAAT PANARFYNQH LINHVGRGTP RHPGAIETYI FAMFNENQKD SGVEQNWGLF 310 YPNMQHVYPI NF

References

[1]	"Primary structure of the (1-3,1-4)-beta-D-glucan 4-glucohydrolase from barley aleurone." Fincher G.B., Lock P.A., Morgan M.M., Lingelbach K., Wettenhall R.E.H., Mercer J.F.B., Brandt A., Thomsen K.K. Proc. Natl. Acad. Sci. U.S.A. 83:2081-2085(1986) [PubMed: 16593676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291, PROTEIN SEQUENCE OF 292-312. Strain: cv. Himalaya.
[2]	"Amino acid sequence homology in two 1,3;1,4-beta-glucan endohydrolases from germinating barley (Hordeum vulgare)." Woodward J.R., Morgan F.J., Fincher G.B. FEBS Lett. 138:198-200(1982) Cited for: PROTEIN SEQUENCE OF 7-46. Strain: cv. Clipper. Tissue: Seed.
[3]	"Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities." Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoej P.B., Fincher G.B. Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994) [PubMed: 8146192] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase." Mueller J.J., Thomsen K.K., Heinemann U. J. Biol. Chem. 273:3438-3446(1998) [PubMed: 9452466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13237 mRNA. Translation: AAA32962.1.

PIR

A25455.

UniGene

Hv.24806

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AQ0	X-ray	2.00	A/B	7-312	[»]
1GHR	X-ray	2.20	A	7-312	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH17. Glycoside Hydrolase Family 17.

Organism-specific databases

Gramene

P12257.

Enzyme and pathway databases

BRENDA

3.2.1.73. 283.

Family and domain databases

InterPro

IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00332. Glyco_hydro_17. 1 hit.
[Graphical view]

PROSITE

PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUB2_HORVU

Accession

Primary (citable) accession number: P12257

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)