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Protein

Endo-beta-N-acetylglucosaminidase F1

Gene

endOF1

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis.

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei182 – 1821Proton 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 F1 (EC:3.2.1.96)
Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1
Endoglycosidase F1
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1
Gene namesi
Name:endOF1
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5050Or 51, or 521 PublicationAdd
BLAST
Chaini51 – 338288Endo-beta-N-acetylglucosaminidase F1PRO_0000011954Add
BLAST
Propeptidei339 – 3391Removed in mature formCuratedPRO_0000011955

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 677Combined sources
Turni68 – 703Combined sources
Helixi73 – 786Combined sources
Beta strandi79 – 813Combined sources
Turni82 – 843Combined sources
Beta strandi91 – 10212Combined sources
Turni103 – 1064Combined sources
Beta strandi107 – 1115Combined sources
Helixi114 – 1218Combined sources
Helixi123 – 1264Combined sources
Helixi128 – 1325Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi145 – 1473Combined sources
Helixi155 – 17218Combined sources
Beta strandi176 – 1805Combined sources
Helixi199 – 21214Combined sources
Beta strandi216 – 2238Combined sources
Helixi224 – 2263Combined sources
Helixi238 – 2403Combined sources
Beta strandi243 – 2475Combined sources
Turni256 – 2583Combined sources
Helixi264 – 2663Combined sources
Beta strandi267 – 2737Combined sources
Turni274 – 2774Combined sources
Helixi282 – 29110Combined sources
Beta strandi295 – 2995Combined sources
Turni306 – 3116Combined sources
Helixi312 – 32413Combined sources
Beta strandi328 – 3303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBNX-ray2.00A51-339[»]
ProteinModelPortaliP36911.
SMRiP36911. Positions 55-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36911.

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.
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.

Sequencei

Sequence statusi: Complete.

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

P36911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFINQFSA SLKNNILVFL AFPFVWTSCA RDNPLSSENS NISPNAAARA
60 70 80 90 100
AVTGTTKANI KLFSFTEVND TNPLNNLNFT LKNSGKPLVD MVVLFSANIN
110 120 130 140 150
YDAANDKVFV SNNPNVQHLL TNRAKYLKPL QDKGIKVILS ILGNHDRSGI
160 170 180 190 200
ANLSTARAKA FAQELKNTCD LYNLDGVFFD DEYSAYQTPP PSGFVTPSNN
210 220 230 240 250
AAARLAYETK QAMPNKLVTV YVYSRTSSFP TAVDGVNAGS YVDYAIHDYG
260 270 280 290 300
GSYDLATNYP GLAKSGMVMS SQEFNQGRYA TAQALRNIVT KGYGGHMIFA
310 320 330
MDPNRSNFTS GQLPALKLIA KELYGDELVY SNTPYSKDW
Length:339
Mass (Da):37,201
Last modified:June 1, 1994 - v1
Checksum:i2EB8D798F9E8CF0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80793 Genomic DNA. Translation: AAA24922.1.
PIRiA42259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80793 Genomic DNA. Translation: AAA24922.1.
PIRiA42259.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBNX-ray2.00A51-339[»]
ProteinModelPortaliP36911.
SMRiP36911. Positions 55-339.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP36911.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
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.
ProtoNetiSearch...

Publicationsi

  1. "Multiple endoglycosidase (Endo) F activities expressed by Flavobacterium meningosepticum. Endo F1: molecular cloning, primary sequence, and structural relationship to Endo H."
    Tarentino A.L., Quinones G., Schrader W.P., Changchien L.-M., Plummer T.H. Jr.
    J. Biol. Chem. 267:3868-3872(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 51-77; 108-161 AND 265-338.
  2. "Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate."
    van Roey P., Rao V., Plummer T.H. Jr., Tarentino A.L.
    Biochemistry 33:13989-13996(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiEBA1_ELIME
AccessioniPrimary (citable) accession number: P36911
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 7, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.