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Protein

Glucan endo-1,3-beta-glucosidase, acidic isoform

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Is thought to be an important plant defense-related product against fungal pathogens.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei259 – 2591NucleophileBy similarity
Active sitei316 – 3161Proton donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. defense response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase, acidic isoform (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
Beta-1,3-endoglucanase
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305: Unplaced

Organism-specific databases

GrameneiP49237.
MaizeGDBi25482.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Chaini30 – 335306Glucan endo-1,3-beta-glucosidase, acidic isoformPRO_0000011854Add
BLAST

Expressioni

Tissue specificityi

Accumulates in aleurone layers. Much lower levels are found in the embryo, and none in starchy endosperm.

Inductioni

By pathogen infection.

Gene expression databases

ExpressionAtlasiP49237. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliP49237.
SMRiP49237. Positions 30-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000238220.

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.

P49237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARQGVIASM HALALLLGAF AAIPTGVQSI GVCYGVNGDN LPPASDVVQL
60 70 80 90 100
YQSNGINLLR IYFPDANPLN ALSGTSIGLI MDVPNTDLAS LASDPSAAAA
110 120 130 140 150
WVQSNVQASR RSACRYIAVG NEVSGGDTGS ILPAMQNLNA ALANAGLGGS
160 170 180 190 200
IKVSTAVQSD VTQGFPPSQG TFSQGYMAPS RQYLQSTGAP LLSNVYPYFS
210 220 230 240 250
YVGNPAQIDL KYALFTSPGT VVQDGSNAYQ NLFDALVDTF VSALEENAGA
260 270 280 290 300
GNVPVVVSES GWPSAGGDAA TAANAQTYNQ NLINHVGQGT PKRPGPIETY
310 320 330
IFAMFNEDQK TGAESERHFG LFNPDKSPVY PINFS
Length:335
Mass (Da):34,894
Last modified:February 1, 1996 - v1
Checksum:i97F89ADF5C4FBA65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95407 mRNA. Translation: AAA74320.1.
PIRiT02088.
RefSeqiNP_001105734.1. NM_001112264.1.
UniGeneiZm.160761.

Genome annotation databases

GeneIDi542755.
KEGGizma:542755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95407 mRNA. Translation: AAA74320.1.
PIRiT02088.
RefSeqiNP_001105734.1. NM_001112264.1.
UniGeneiZm.160761.

3D structure databases

ProteinModelPortaliP49237.
SMRiP49237. Positions 30-334.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi542755.
KEGGizma:542755.

Organism-specific databases

GrameneiP49237.
MaizeGDBi25482.

Phylogenomic databases

HOGENOMiHOG000238220.

Gene expression databases

ExpressionAtlasiP49237. baseline and differential.

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. "Nucleotide sequence of a maize cDNA for a class II, acidic beta-1,3-glucanase."
    Wu S., Kriz A.L., Widholm J.M.
    Plant Physiol. 106:1709-1710(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Va26.
    Tissue: Seedling.

Entry informationi

Entry nameiE13B_MAIZE
AccessioniPrimary (citable) accession number: P49237
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 4, 2015
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.