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Protein

Lichenase-2

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues.

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei238 – 2381Nucleophile
Active sitei294 – 2941Proton donor

GO - Molecular functioni

  1. licheninase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00350.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP12257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 6›61 Publication
Chaini7 – 312306Lichenase-2PRO_0000011897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi196 – 1961N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Expressioni

Gene expression databases

ExpressionAtlasiP12257. baseline.
GenevestigatoriP12257.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi21 – 3111Combined sources
Beta strandi35 – 406Combined sources
Helixi43 – 497Combined sources
Beta strandi55 – 606Combined sources
Helixi62 – 643Combined sources
Helixi65 – 706Combined sources
Helixi72 – 8211Combined sources
Turni83 – 853Combined sources
Beta strandi89 – 9911Combined sources
Helixi102 – 1076Combined sources
Helixi108 – 12114Combined sources
Beta strandi127 – 1348Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Helixi144 – 1463Combined sources
Helixi151 – 16717Combined sources
Beta strandi171 – 1744Combined sources
Helixi177 – 1837Combined sources
Turni185 – 1873Combined sources
Helixi190 – 1945Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi207 – 2093Combined sources
Helixi212 – 22514Combined sources
Turni226 – 2283Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi243 – 2464Combined sources
Helixi251 – 26414Combined sources
Turni265 – 2673Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi278 – 2814Combined sources
Helixi293 – 2953Combined sources
Beta strandi306 – 3083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ0X-ray2.00A/B7-312[»]
1GHRX-ray2.20A7-312[»]
ProteinModelPortaliP12257.
SMRiP12257. Positions 7-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12257.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PPSVESIGVC YGMSANNLPA ASTVVSMFKF NGIKSMRLYA PNQAALQAVG
60 70 80 90 100
GTGINVVVGA PNDVLSNLAA SPAAAASWVK SNIQAYPKVS FRYVCVGNEV
110 120 130 140 150
AGGATRNLVP AMKNVHGALV AAGLGHIKVT TSVSQAILGV FSPPSAGSFT
160 170 180 190 200
GEAAAFMGPV VQFLARTNAP LMANIYPYLA WAYNPSAMDM GYALFNASGT
210 220 230 240 250
VVRDGAYGYQ NLFDTTVDAF YTAMGKHGGS SVKLVVSESG WPSGGGTAAT
260 270 280 290 300
PANARFYNQH LINHVGRGTP RHPGAIETYI FAMFNENQKD SGVEQNWGLF
310
YPNMQHVYPI NF
Length:312
Mass (Da):32,774
Last modified:September 30, 1989 - v1
Checksum:i7D18C2A6DF522E17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13237 mRNA. Translation: AAA32962.1.
PIRiA25455.
UniGeneiHv.24806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13237 mRNA. Translation: AAA32962.1.
PIRiA25455.
UniGeneiHv.24806.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ0X-ray2.00A/B7-312[»]
1GHRX-ray2.20A7-312[»]
ProteinModelPortaliP12257.
SMRiP12257. Positions 7-312.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP12257.

Enzyme and pathway databases

UniPathwayiUPA00350.

Miscellaneous databases

EvolutionaryTraceiP12257.

Gene expression databases

ExpressionAtlasiP12257. baseline.
GenevestigatoriP12257.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1985) [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(1981)
    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(1993) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiGUB2_HORVU
AccessioniPrimary (citable) accession number: P12257
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1989
Last sequence update: September 30, 1989
Last modified: January 6, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.