ID EBA3_ELIME Reviewed; 329 AA. AC P36913; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 22-FEB-2023, entry version 113. DE RecName: Full=Endo-beta-N-acetylglucosaminidase F3; DE EC=3.2.1.96; DE AltName: Full=Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3; DE AltName: Full=Endoglycosidase F3; DE AltName: Full=Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3; DE Flags: Precursor; GN Name=endOF3; OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Elizabethkingia. OX NCBI_TaxID=238; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8486657; DOI=10.1016/s0021-9258(18)98405-x; RA Tarentino A.L., Quinones G., Changchien L.-M., Plummer T.H. Jr.; RT "Multiple endoglycosidase F activities expressed by Flavobacterium RT meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary RT sequence, and enzyme expression."; RL J. Biol. Chem. 268:9702-9708(1993). RN [2] RP GLYCOSYLATION AT THR-88, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=7768916; DOI=10.1074/jbc.270.22.13192; RA Plummer T.H. Jr., Tarentino A.L., Hauer C.R.; RT "Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum RT proteins. Asp-Ser and Asp-Thr-Thr consensus sites."; RL J. Biol. Chem. 270:13192-13196(1995). RN [3] RP STRUCTURE OF CARBOHYDRATE, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=7768917; DOI=10.1074/jbc.270.22.13197; RA Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N.; RT "Detailed structural analysis of a novel, specific O-linked glycan from the RT prokaryote Flavobacterium meningosepticum."; RL J. Biol. Chem. 270:13197-13203(1995). CC -!- FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high- CC mannose glycopeptides and glycoproteins. Hydrolyzes bi- and CC triantennary glycans. The presence of a core-bound fucose greatly CC augments endo F3 activity on biantennary and, presumably, triantennary CC oligosaccharides. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta- CC D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl- CC [protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]- CC beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L- CC asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603, CC Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248, CC ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; EC=3.2.1.96; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Carbohydrate at Thr-88 consists of (2-OMe)Man1-4GlcNAcU1-4GlcU1- CC 4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L06332; AAA24924.1; -; Genomic_DNA. DR PIR; B46678; B46678. DR PDB; 1EOK; X-ray; 1.80 A; A=40-329. DR PDB; 1EOM; X-ray; 2.10 A; A=40-329. DR PDBsum; 1EOK; -. DR PDBsum; 1EOM; -. DR AlphaFoldDB; P36913; -. DR SMR; P36913; -. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR GlyCosmos; P36913; 1 site, No reported glycans. DR iPTMnet; P36913; -. DR EvolutionaryTrace; P36913; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd06542; GH18_EndoS-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS51910; GH18_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Glycosidase; KW Hydrolase; Secreted; Signal. FT SIGNAL 1..39 FT /note="Or 40, or 41" FT CHAIN 40..329 FT /note="Endo-beta-N-acetylglucosaminidase F3" FT /id="PRO_0000011957" FT DOMAIN 48..329 FT /note="GH18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT ACT_SITE 167 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258" FT CARBOHYD 88 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:7768916" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1EOM" FT HELIX 104..115 FT /evidence="ECO:0007829|PDB:1EOK" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:1EOK" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:1EOM" FT HELIX 199..208 FT /evidence="ECO:0007829|PDB:1EOK" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 233..240 FT /evidence="ECO:0007829|PDB:1EOK" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 256..268 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:1EOK" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 289..297 FT /evidence="ECO:0007829|PDB:1EOK" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:1EOK" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:1EOK" SQ SEQUENCE 329 AA; 35844 MW; C12EA4C8920784FF CRC64; MKKIFFAQCS ILLLMLGSCS KMTEDMTPES VNKEASVKSA TALAGSNGVC IAYYITDGRN PTFKLKDIPD KVDMVILFGL KYWSLQDTTK LPGGTGMMGS FKSYKDLDTQ IRSLQSRGIK VLQNIDDDVS WQSSKPGGFA SAAAYGDAIK SIVIDKWKLD GISLDIEHSG AKPNPIPTFP GYAATGYNGW YSGSMAATPA FLNVISELTK YFGTTAPNNK QLQIASGIDV YAWNKIMENF RNNFNYIQLQ SYGANVSRTQ LMMNYATGTN KIPASKMVFG AYAEGGTNQA NDVEVAKWTP TQGAKGGMMI YTYNSNVSYA NAVRDAVKN //