EBA3_ELIME
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 03-AUG-2022, entry version 110.
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; Bacteroidetes; 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=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins containing the
CC -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC remains attached to the protein, the rest of the oligosaccharide is
CC released intact.; 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}.
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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 iPTMnet; P36913; -.
DR PRIDE; 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 InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 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
