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P80036 (EBAG_FLAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismFlavobacterium sp. (strain SK1022)
Taxonomic identifier148444 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subunit structure

Monomer.

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0-9.0. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4747 Ref.2
Chain48 – 314267Endo-beta-N-acetylglucosaminidase
PRO_0000077053

Sites

Active site1751Proton donor
Site1741Important for substrate specificity

Experimental info

Mutagenesis601Y → A: Reduced catalytic activity. Ref.1
Mutagenesis1681D → N: Loss of catalytic activity. Ref.1
Mutagenesis1691G → L: Reduced catalytic activity. Ref.1
Mutagenesis1731D → E or N: Reduced catalytic activity. Ref.1
Mutagenesis1741D → E or N: Reduced catalytic activity toward hybrid type oligosaccharides. Ref.1
Mutagenesis1751E → A: Loss of catalytic activity. Ref.1
Mutagenesis2381Y → A: Reduced catalytic activity. Ref.1
Sequence conflict1941W → G AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P80036 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 0227CD75BE4DC5BF

FASTA31432,936
        10         20         30         40         50         60 
MQFGIVAAIA DGGRTARAGG SVRPPRRPPA SHTAWGLPRG RPTGQPHATP TKSGPTSIAY 

        70         80         90        100        110        120 
VEVNNDQLAN VGRYQLANGA NAFDVAIIFA ANINWNGSKA VLYNNENVQA TLDDAATQIR 

       130        140        150        160        170        180 
PLQAKGIKVS LSILGNHQGA GIANFPTQAA AEDFAAQVSA TVSKYGLDGV DLDDEYSDYG 

       190        200        210        220        230        240 
TNGTPQPNQQ SIGWLISALR ADVPGKLISF YDIGPASSAL SSSSSTIGSK LDYAWNPYYG 

       250        260        270        280        290        300 
TYSAPSIPGL DKSRLSAAAV DVQNTPQSTA VSLAQRTKAD GYGVFMTYNL PDGDVSPYVS 

       310 
SMTKVLYGQA ATYH

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB053207 Genomic DNA. Translation: BAB20938.1.
PIRS19538.

3D structure databases

ProteinModelPortalP80036.
SMRP80036. Positions 52-311.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR016289. Glyco_hydro_18_end-b-GlcNAcase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PIRSFPIRSF001103. Endo-b-N-acetylglucosaminidase. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEBAG_FLAST
AccessionPrimary (citable) accession number: P80036
Secondary accession number(s): Q9F1K1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 15, 2008
Last modified: May 1, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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