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P12257 (GUB2_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lichenase-2

EC=3.2.1.73
Alternative name(s):
(1->3,1->4)-beta-glucanase isoenzyme EII
Endo-beta-1,3-1,4 glucanase II
Lichenase II
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length312 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionlicheninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 6›6 Ref.2
Chain7 – 312306Lichenase-2
PRO_0000011897

Sites

Active site2381Nucleophile
Active site2941Proton donor

Amino acid modifications

Glycosylation1961N-linked (GlcNAc...)

Experimental info

Non-terminal residue11

Secondary structure

............................................................ 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12257 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 7D18C2A6DF522E17

FASTA31232,774
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13237 mRNA. Translation: AAA32962.1.
PIRA25455.
UniGeneHv.24806.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ0X-ray2.00A/B7-312[»]
1GHRX-ray2.20A7-312[»]
ProteinModelPortalP12257.
SMRP12257. Positions 7-312.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP12257.

Enzyme and pathway databases

UniPathwayUPA00350.

Gene expression databases

GenevestigatorP12257.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12257.

Entry information

Entry nameGUB2_HORVU
AccessionPrimary (citable) accession number: P12257
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries