ID   EBAG_FLAST              Reviewed;         314 AA.
AC   P80036; Q9F1K1;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   22-FEB-2023, entry version 82.
DE   RecName: Full=Endo-beta-N-acetylglucosaminidase;
DE            EC=3.2.1.96;
DE   AltName: Full=DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase;
DE   AltName: Full=Endo-Fsp;
DE   AltName: Full=Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase;
DE   Flags: Precursor;
OS   Flavobacterium sp. (strain SK1022).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=148444;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP   TYR-60; ASP-168; GLY-169; ASP-173; ASP-174; GLU-175 AND TYR-238.
RX   PubMed=11515537; DOI=10.1271/bbb.65.1542;
RA   Fujita K., Nakatake R., Yamabe K., Watanabe A., Asada Y., Takegawa K.;
RT   "Identification of amino acid residues essential for the substrate
RT   specificity of Flavobacterium sp. endo-beta-N-acetylglucosaminidase.";
RL   Biosci. Biotechnol. Biochem. 65:1542-1548(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-314.
RX   PubMed=1935974; DOI=10.1111/j.1432-1033.1991.tb16359.x;
RA   Takegawa K., Mikami B., Iwahara S., Morita Y., Yamamoto K., Tochikura T.;
RT   "Complete amino acid sequence of endo-beta-N-acetylglucosaminidase from
RT   Flavobacterium sp.";
RL   Eur. J. Biochem. 202:175-180(1991).
CC   -!- FUNCTION: Cleaves asparagine-linked oligomannose and hybrid, but not
CC       complex, oligosaccharides from glycoproteins.
CC       {ECO:0000269|PubMed:11515537}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0-9.0. {ECO:0000269|PubMed:11515537};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11515537}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; AB053207; BAB20938.1; -; Genomic_DNA.
DR   PIR; S19538; S19538.
DR   AlphaFoldDB; P80036; -.
DR   SMR; P80036; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
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; IPR016289; Endo-Fsp.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   PIRSF; PIRSF001103; Endo-b-N-acetylglucosaminidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000269|PubMed:1935974"
FT   CHAIN           48..314
FT                   /note="Endo-beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000077053"
FT   DOMAIN          55..309
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          14..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   SITE            174
FT                   /note="Important for substrate specificity"
FT   MUTAGEN         60
FT                   /note="Y->A: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         168
FT                   /note="D->N: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         169
FT                   /note="G->L: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         173
FT                   /note="D->E,N: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         174
FT                   /note="D->E,N: Reduced catalytic activity toward hybrid
FT                   type oligosaccharides."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         175
FT                   /note="E->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   MUTAGEN         238
FT                   /note="Y->A: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11515537"
FT   CONFLICT        194
FT                   /note="W -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  32936 MW;  0227CD75BE4DC5BF CRC64;
     MQFGIVAAIA DGGRTARAGG SVRPPRRPPA SHTAWGLPRG RPTGQPHATP TKSGPTSIAY
     VEVNNDQLAN VGRYQLANGA NAFDVAIIFA ANINWNGSKA VLYNNENVQA TLDDAATQIR
     PLQAKGIKVS LSILGNHQGA GIANFPTQAA AEDFAAQVSA TVSKYGLDGV DLDDEYSDYG
     TNGTPQPNQQ SIGWLISALR ADVPGKLISF YDIGPASSAL SSSSSTIGSK LDYAWNPYYG
     TYSAPSIPGL DKSRLSAAAV DVQNTPQSTA VSLAQRTKAD GYGVFMTYNL PDGDVSPYVS
     SMTKVLYGQA ATYH
//