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Protein

Endoglycoceramidase

Gene
N/A
Organism
Cyanea nozakii (Jellyfish)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolysis of the glycosidic linkage between oligosaccharides and ceramides of glycosphingolipids, especially b-series polysialogangliosides.1 Publication

Catalytic activityi

Oligoglycosylglucosyl-(1<->1)-ceramide + H2O = ceramide + oligoglycosylglucose.1 Publication

Enzyme regulationi

Completely inhibited by Hg2+. Cu2+ and zinc have no effect on enzyme activity. Lithium, potassium, manganese, Ni2+, calcium, magnesium and EDTA have no significant effect on enzyme activity. Enzyme requires presence of detergents such as Triton X-100 and Lubrol PX for the hydrolysis of glycosphingolipids. Taurodeoxycholate strongly inhibits the enzyme activity and SDS completely inhibits the enzyme activity.1 Publication

Kineticsi

  1. KM=0.35 mM for GM11 Publication
  1. Vmax=4.4 µM/min/mg enzyme1 Publication

pH dependencei

Optimum pH 3.0. Highly stable at acidic pH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei239Proton donorSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.123. 1767.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
EndoglycoceramidaseImported (EC:3.2.1.123)
Short name:
EGCase1 Publication
Alternative name(s):
Glycosphingolipid-specific enzyme1 Publication
Short name:
GSL-specific enzyme1 Publication
OrganismiCyanea nozakii (Jellyfish)
Taxonomic identifieri135523 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaScyphozoaSemaeostomeaeCyaneidaeCyanea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000039038122 – 503EndoglycoceramidaseSequence analysisAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi72N-linked (GlcNAc...)1 Publication1
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Glycosylationi205N-linked (GlcNAc...)Sequence analysis1
Glycosylationi307N-linked (GlcNAc...)1 Publication1
Glycosylationi409N-linked (GlcNAc...)Sequence analysis1
Glycosylationi485N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9GV16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 5 (cellulase A) family.Sequence analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9GV16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETQPLVFV LMSISAILTA GLPINDDASL LISVNPETQQ LVDSLGRERF
60 70 80 90 100
FHGTNVVVKH KPYHPSVEGY DNTSFSEVDM KILQDLGLNT IRLGMMLPGY
110 120 130 140 150
VPTRGNYNET YLKIIQEIVS KAAKYGIYTL LDMHQDVMSA KFCVEGFPDW
160 170 180 190 200
AVNTGNADNF PFPLEDKYPL NLQTGYPYPK DCAKHAWGDY YFTEAAAAAF
210 220 230 240 250
QNFYNNTDGL LDAWADFWKK TAQGFKDYKS VIGYELINEP FAGDIYRDPS
260 270 280 290 300
LMIPGVADER NLAPAYDVIH KAIRTVDEQH SIFFEGVTWD YFAAGFSKVP
310 320 330 340 350
GGDAYRNRSV LSYHYYEPPD FNKKFQFEVR MEDLRRLKCG GFLTELLTVG
360 370 380 390 400
DTAKDMSDML ELFDICDQHK QSWMGWLYKS YGCYKQHLGC LTDSMHDETG
410 420 430 440 450
HLRDIVLQNT TRTYPQAVAG HTIGYKFDRI TKKFDLSFVV TADCRSTESI
460 470 480 490 500
VYFNKDLHYS NGYDVTVFPK DSVTWKQVEK KIIINHSQKL SAGTTVTFSL

VAK
Length:503
Mass (Da):57,253
Last modified:March 1, 2001 - v1
Checksum:i3383E64987E7B15A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti172L → P.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047321 mRNA. Translation: BAB16369.1.
AB047322 mRNA. Translation: BAB16370.1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047321 mRNA. Translation: BAB16369.1.
AB047322 mRNA. Translation: BAB16370.1.

3D structure databases

ProteinModelPortaliQ9GV16.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.123. 1767.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEGCSE_CYANO
AccessioniPrimary (citable) accession number: Q9GV16
Secondary accession number(s): Q9GV15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

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