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P36911

- EBA1_ELIME

UniProt

P36911 - EBA1_ELIME

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Protein

Endo-beta-N-acetylglucosaminidase F1

Gene

endOF1

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - 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-KW
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 – 677
Turni68 – 703
Helixi73 – 786
Beta strandi79 – 813
Turni82 – 843
Beta strandi91 – 10212
Turni103 – 1064
Beta strandi107 – 1115
Helixi114 – 1218
Helixi123 – 1264
Helixi128 – 1325
Beta strandi136 – 1427
Beta strandi145 – 1473
Helixi155 – 17218
Beta strandi176 – 1805
Helixi199 – 21214
Beta strandi216 – 2238
Helixi224 – 2263
Helixi238 – 2403
Beta strandi243 – 2475
Turni256 – 2583
Helixi264 – 2663
Beta strandi267 – 2737
Turni274 – 2774
Helixi282 – 29110
Beta strandi295 – 2995
Turni306 – 3116
Helixi312 – 32413
Beta strandi328 – 3303

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
M80793 Genomic DNA. Translation: AAA24922.1.
PIRiA42259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M80793 Genomic DNA. Translation: AAA24922.1 .
PIRi A42259.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EBN X-ray 2.00 A 51-339 [» ]
ProteinModelPortali P36911.
SMRi P36911. Positions 55-339.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P36911.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR016289. Endo-Fsp.
IPR001223. Glyco_hydro18cat.
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.
ProtoNeti Search...

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: October 29, 2014
This is version 86 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