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Protein

Lichenase-2

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

Keywordsi

Molecular functionGlycosidase, 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...) asparagine1

Keywords - PTMi

Glycoprotein

Expressioni

Gene expression databases

ExpressionAtlasiP12257 baseline and differential

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

InterProiView protein in InterPro
IPR000490 Glyco_hydro_17
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00332 Glyco_hydro_17, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00587 GLYCOSYL_HYDROL_F17, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGUB2_HORVU
AccessioniPrimary (citable) accession number: P12257
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 23, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health