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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: beta-D-glucan degradation

This protein is involved in the pathway beta-D-glucan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway beta-D-glucan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei238Nucleophile1
Active sitei294Proton donor1

GO - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 61 Publication›6
ChainiPRO_00000118977 – 312Lichenase-2Add BLAST306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi196N-linked (GlcNAc...)1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi21 – 31Combined sources11
Beta strandi35 – 40Combined sources6
Helixi43 – 49Combined sources7
Beta strandi55 – 60Combined sources6
Helixi62 – 64Combined sources3
Helixi65 – 70Combined sources6
Helixi72 – 82Combined sources11
Turni83 – 85Combined sources3
Beta strandi89 – 99Combined sources11
Helixi102 – 107Combined sources6
Helixi108 – 121Combined sources14
Beta strandi127 – 134Combined sources8
Helixi135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Helixi144 – 146Combined sources3
Helixi151 – 167Combined sources17
Beta strandi171 – 174Combined sources4
Helixi177 – 183Combined sources7
Turni185 – 187Combined sources3
Helixi190 – 194Combined sources5
Beta strandi201 – 204Combined sources4
Beta strandi207 – 209Combined sources3
Helixi212 – 225Combined sources14
Turni226 – 228Combined sources3
Beta strandi234 – 238Combined sources5
Beta strandi243 – 246Combined sources4
Helixi251 – 264Combined sources14
Turni265 – 267Combined sources3
Beta strandi270 – 274Combined sources5
Beta strandi278 – 281Combined sources4
Helixi293 – 295Combined sources3
Beta strandi306 – 308Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP12257.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IH05. Eukaryota.
ENOG410YAHP. LUCA.

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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AQ0X-ray2.00A/B7-312[»]
1GHRX-ray2.20A7-312[»]
ProteinModelPortaliP12257.
SMRiP12257.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IH05. Eukaryota.
ENOG410YAHP. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00350.

Miscellaneous databases

EvolutionaryTraceiP12257.

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...

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: November 2, 2016
This is version 104 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

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 one 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.