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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)DescriptionActionsGraphical viewLength
Active sitei182Proton donor1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 50Or 51, or 521 PublicationAdd BLAST50
ChainiPRO_000001195451 – 338Endo-beta-N-acetylglucosaminidase F1Add BLAST288
PropeptideiPRO_0000011955339Removed in mature formCurated1

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 67Combined sources7
Turni68 – 70Combined sources3
Helixi73 – 78Combined sources6
Beta strandi79 – 81Combined sources3
Turni82 – 84Combined sources3
Beta strandi91 – 102Combined sources12
Turni103 – 106Combined sources4
Beta strandi107 – 111Combined sources5
Helixi114 – 121Combined sources8
Helixi123 – 126Combined sources4
Helixi128 – 132Combined sources5
Beta strandi136 – 142Combined sources7
Beta strandi145 – 147Combined sources3
Helixi155 – 172Combined sources18
Beta strandi176 – 180Combined sources5
Helixi199 – 212Combined sources14
Beta strandi216 – 223Combined sources8
Helixi224 – 226Combined sources3
Helixi238 – 240Combined sources3
Beta strandi243 – 247Combined sources5
Turni256 – 258Combined sources3
Helixi264 – 266Combined sources3
Beta strandi267 – 273Combined sources7
Turni274 – 277Combined sources4
Helixi282 – 291Combined sources10
Beta strandi295 – 299Combined sources5
Turni306 – 311Combined sources6
Helixi312 – 324Combined sources13
Beta strandi328 – 330Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBNX-ray2.00A51-339[»]
ProteinModelPortaliP36911.
SMRiP36911.
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_hydro18_cat.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBNX-ray2.00A51-339[»]
ProteinModelPortaliP36911.
SMRiP36911.
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_hydro18_cat.
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...

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: November 2, 2016
This is version 92 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

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 one 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.