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Protein

Glucan endo-1,3-beta-glucosidase GII

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

Functioni

May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides (PubMed:1899089). Hydrolyzes laminarin in vitro (PubMed:8514770).2 Publications

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.1 Publication

pH dependencei

Optimum pH is 4.5 (at 37 degrees Celsius).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei259Nucleophile1 Publication1
Active sitei316Proton donor1 Publication1

GO - Molecular functioni

  • glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB

GO - Biological processi

  • (1->3)-beta-D-glucan catabolic process Source: UniProtKB
  • defense response to fungus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

SABIO-RKP15737.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase GII (EC:3.2.1.391 Publication)
Alternative name(s):
(1->3)-beta-glucan endohydrolase GII
(1->3)-beta-glucanase isoenzyme GII
Beta-1,3-endoglucanase GII
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 282 PublicationsAdd BLAST28
ChainiPRO_000001184829 – 334Glucan endo-1,3-beta-glucosidase GIIAdd BLAST306

Proteomic databases

PRIDEiP15737.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi37 – 39Combined sources3
Helixi43 – 53Combined sources11
Beta strandi57 – 62Combined sources6
Helixi65 – 70Combined sources6
Turni71 – 73Combined sources3
Beta strandi77 – 81Combined sources5
Helixi84 – 86Combined sources3
Helixi87 – 92Combined sources6
Helixi94 – 104Combined sources11
Turni105 – 111Combined sources7
Beta strandi112 – 122Combined sources11
Helixi125 – 130Combined sources6
Helixi131 – 145Combined sources15
Beta strandi150 – 157Combined sources8
Helixi158 – 160Combined sources3
Helixi167 – 169Combined sources3
Beta strandi171 – 174Combined sources4
Helixi176 – 187Combined sources12
Beta strandi191 – 194Combined sources4
Helixi197 – 203Combined sources7
Turni205 – 207Combined sources3
Helixi210 – 214Combined sources5
Turni224 – 226Combined sources3
Helixi233 – 248Combined sources16
Beta strandi255 – 260Combined sources6
Beta strandi264 – 267Combined sources4
Helixi272 – 283Combined sources12
Helixi286 – 288Combined sources3
Beta strandi299 – 302Combined sources4
Helixi314 – 318Combined sources5
Beta strandi328 – 330Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortaliP15737.
SMRiP15737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15737.

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: Complete.

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

P15737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKDVASMF AAALFIGAFA AVPTSVQSIG VCYGVIGNNL PSRSDVVQLY
60 70 80 90 100
RSKGINGMRI YFADGQALSA LRNSGIGLIL DIGNDQLANI AASTSNAASW
110 120 130 140 150
VQNNVRPYYP AVNIKYIAAG NEVQGGATQS ILPAMRNLNA ALSAAGLGAI
160 170 180 190 200
KVSTSIRFDE VANSFPPSAG VFKNAYMTDV ARLLASTGAP LLANVYPYFA
210 220 230 240 250
YRDNPGSISL NYATFQPGTT VRDQNNGLTY TSLFDAMVDA VYAALEKAGA
260 270 280 290 300
PAVKVVVSES GWPSAGGFAA SAGNARTYNQ GLINHVGGGT PKKREALETY
310 320 330
IFAMFNENQK TGDATERSFG LFNPDKSPAY NIQF
Length:334
Mass (Da):35,194
Last modified:April 1, 1990 - v1
Checksum:i552D66A29A08C703
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12A → V in AAA32939 (PubMed:1899089).Curated1
Sequence conflicti71L → V in AAA32939 (PubMed:1899089).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62907 mRNA. Translation: AAA32939.1.
X16274 mRNA. Translation: CAA34350.1.
M23548 mRNA. Translation: AAA32958.1.
PIRiS05510.
UniGeneiHv.18110.
Hv.25599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62907 mRNA. Translation: AAA32939.1.
X16274 mRNA. Translation: CAA34350.1.
M23548 mRNA. Translation: AAA32958.1.
PIRiS05510.
UniGeneiHv.18110.
Hv.25599.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortaliP15737.
SMRiP15737.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEiP15737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IH05. Eukaryota.
ENOG410YAHP. LUCA.

Enzyme and pathway databases

SABIO-RKP15737.

Miscellaneous databases

EvolutionaryTraceiP15737.

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 nameiE13B_HORVU
AccessioniPrimary (citable) accession number: P15737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 102 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.