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P12257

- GUB2_HORVU

UniProt

P12257 - GUB2_HORVU

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Protein

Lichenase-2

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed - 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

GenevestigatoriP12257.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:October 1, 1989 - v1
Checksum:i7D18C2A6DF522E17
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13237 mRNA. Translation: AAA32962.1.
PIRiA25455.
UniGeneiHv.24806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13237 mRNA. Translation: AAA32962.1 .
PIRi A25455.
UniGenei Hv.24806.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AQ0 X-ray 2.00 A/B 7-312 [» ]
1GHR X-ray 2.20 A 7-312 [» ]
ProteinModelPortali P12257.
SMRi P12257. Positions 7-312.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P12257.

Enzyme and pathway databases

UniPathwayi UPA00350 .

Miscellaneous databases

EvolutionaryTracei P12257.

Gene expression databases

Genevestigatori P12257.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00332. Glyco_hydro_17. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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).

Entry informationi

Entry nameiGUB2_HORVU
AccessioniPrimary (citable) accession number: P12257
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 1, 2014
This is version 92 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