Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-beta-N-acetylglucosaminidase F2

Gene

endOF2

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Complex biantennary glycans are the preferred substrates. Tri- and tetraantennary glycans are not hydrolyzed, and high mannose glycans are very poor substrates.

Catalytic activityi

Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei171Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase

Protein family/group databases

CAZyiGH18 Glycoside Hydrolase Family 18

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-N-acetylglucosaminidase F2 (EC:3.2.1.96)
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
Endoglycosidase F2
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2
Gene namesi
Name:endOF2
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 45Add BLAST45
ChainiPRO_000001195646 – 335Endo-beta-N-acetylglucosaminidase F2Add BLAST290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi73O-linked (Man...) serine1 Publication1
Glycosylationi89O-linked (Man...) serine1 Publication1
Glycosylationi143O-linked (Man...) serine1 Publication1

Post-translational modificationi

Carbohydrates at Ser-73, Ser-89 and Ser-143 consist of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnetiP36912

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP36912
SMRiP36912
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS01095 CHITINASE_18, 1 hit

Sequencei

Sequence statusi: Complete.

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

P36912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTANFSFAL CLSVVIMLFI KCTRSEQDLS VTKDAIAQKS GVTVSAVNLS
60 70 80 90 100
NLIAYKNSDH QISAGYYRTW RDSATASGNL PSMRWLPDSL DMVMVFPDYT
110 120 130 140 150
PPENAYWNTL KTNYVPYLHK RGTKVIITLG DLNSATTTGG QDSIGYSSWA
160 170 180 190 200
KGIYDKWVGE YNLDGIDIDI ESSPSGATLT KFVAATKALS KYFGPKSGTG
210 220 230 240 250
KTFVYDTNQN PTNFFIQTAP RYNYVFLQAY GRSTTNLTTV SGLYAPYISM
260 270 280 290 300
KQFLPGFSFY EENGYPGNYW NDVRYPQNGT GRAYDYARWQ PATGKKGGVF
310 320 330
SYAIERDAPL TSSNDNTLRA PNFRVTKDLI KIMNP
Length:335
Mass (Da):37,356
Last modified:June 1, 1994 - v1
Checksum:iFBAD1228C75F1CAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06331 Genomic DNA Translation: AAA24923.1
PIRiA46678

Similar proteinsi

Entry informationi

Entry nameiEBA2_ELIME
AccessioniPrimary (citable) accession number: P36912
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 25, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health