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Protein

Endo-beta-N-acetylglucosaminidase

Gene
N/A
Organism
Flavobacterium sp. (strain SK1022)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.1 Publication

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.

pH dependencei

Optimum pH is 5.0-9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei174 – 1741Important for substrate specificity
Active sitei175 – 1751Proton donor

GO - Molecular functioni

  1. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
Alternative name(s):
DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase
Endo-Fsp
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase
OrganismiFlavobacterium sp. (strain SK1022)
Taxonomic identifieri148444 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601Y → A: Reduced catalytic activity. 1 Publication
Mutagenesisi168 – 1681D → N: Loss of catalytic activity. 1 Publication
Mutagenesisi169 – 1691G → L: Reduced catalytic activity. 1 Publication
Mutagenesisi173 – 1731D → E or N: Reduced catalytic activity. 1 Publication
Mutagenesisi174 – 1741D → E or N: Reduced catalytic activity toward hybrid type oligosaccharides. 1 Publication
Mutagenesisi175 – 1751E → A: Loss of catalytic activity. 1 Publication
Mutagenesisi238 – 2381Y → A: Reduced catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 47471 PublicationAdd
BLAST
Chaini48 – 314267Endo-beta-N-acetylglucosaminidasePRO_0000077053Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP80036.
SMRiP80036. Positions 52-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFiPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80036-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFGIVAAIA DGGRTARAGG SVRPPRRPPA SHTAWGLPRG RPTGQPHATP
60 70 80 90 100
TKSGPTSIAY VEVNNDQLAN VGRYQLANGA NAFDVAIIFA ANINWNGSKA
110 120 130 140 150
VLYNNENVQA TLDDAATQIR PLQAKGIKVS LSILGNHQGA GIANFPTQAA
160 170 180 190 200
AEDFAAQVSA TVSKYGLDGV DLDDEYSDYG TNGTPQPNQQ SIGWLISALR
210 220 230 240 250
ADVPGKLISF YDIGPASSAL SSSSSTIGSK LDYAWNPYYG TYSAPSIPGL
260 270 280 290 300
DKSRLSAAAV DVQNTPQSTA VSLAQRTKAD GYGVFMTYNL PDGDVSPYVS
310
SMTKVLYGQA ATYH
Length:314
Mass (Da):32,936
Last modified:January 14, 2008 - v2
Checksum:i0227CD75BE4DC5BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941W → G AA sequence (PubMed:1935974).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053207 Genomic DNA. Translation: BAB20938.1.
PIRiS19538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053207 Genomic DNA. Translation: BAB20938.1.
PIRiS19538.

3D structure databases

ProteinModelPortaliP80036.
SMRiP80036. Positions 52-311.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFiPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of amino acid residues essential for the substrate specificity of Flavobacterium sp. endo-beta-N-acetylglucosaminidase."
    Fujita K., Nakatake R., Yamabe K., Watanabe A., Asada Y., Takegawa K.
    Biosci. Biotechnol. Biochem. 65:1542-1548(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, MUTAGENESIS OF TYR-60; ASP-168; GLY-169; ASP-173; ASP-174; GLU-175 AND TYR-238.
  2. "Complete amino acid sequence of endo-beta-N-acetylglucosaminidase from Flavobacterium sp."
    Takegawa K., Mikami B., Iwahara S., Morita Y., Yamamoto K., Tochikura T.
    Eur. J. Biochem. 202:175-180(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-314.

Entry informationi

Entry nameiEBAG_FLAST
AccessioniPrimary (citable) accession number: P80036
Secondary accession number(s): Q9F1K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1991
Last sequence update: January 14, 2008
Last modified: January 6, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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.