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P80036

- EBAG_FLAST

UniProt

P80036 - EBAG_FLAST

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Protein

Endo-beta-N-acetylglucosaminidase

Gene
N/A
Organism
Flavobacterium sp. (strain SK1022)
Status
Reviewed - 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-KW
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 15, 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:
EMBL
GenBank
DDBJ
Links Updated
AB053207 Genomic DNA. Translation: BAB20938.1.
PIRiS19538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB053207 Genomic DNA. Translation: BAB20938.1 .
PIRi S19538.

3D structure databases

ProteinModelPortali P80036.
SMRi P80036. Positions 52-311.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
PIRSFi PIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2001) [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(1991) [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: November 1, 1991
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 65 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