EBAG_STRPL
ID EBAG_STRPL Reviewed; 313 AA.
AC P04067;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Endo-beta-N-acetylglucosaminidase H;
DE EC=3.2.1.96;
DE AltName: Full=DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase H;
DE AltName: Full=Endoglycosidase H;
DE Short=Endo H;
DE AltName: Full=Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase H;
DE Flags: Precursor;
OS Streptomyces plicatus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces rochei group.
OX NCBI_TaxID=1922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6429133; DOI=10.1016/s0021-9258(17)42829-8;
RA Robbins P.W., Trimble R.B., Wirth D.F., Hering C., Maley F., Maley G.F.,
RA Das R., Gibson B.W., Royal N., Biemann K.;
RT "Primary structure of the Streptomyces enzyme endo-beta-N-
RT acetylglucosaminidase H.";
RL J. Biol. Chem. 259:7577-7583(1984).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 43-313, AND FUNCTION.
RX PubMed=7663942; DOI=10.1016/s0969-2126(01)00178-2;
RA Rao V., Guan C., Van Roey P.;
RT "Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9-A
RT resolution: active-site geometry and substrate recognition.";
RL Structure 3:449-457(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 48-312 OF MUTANTS, FUNCTION,
RP PROBABLE ACTIVE SITE, AND MUTAGENESIS OF ASP-172 AND GLU-174.
RX PubMed=10595536; DOI=10.1110/ps.8.11.2338;
RA Rao V., Cui T., Guan C., Van Roey P.;
RT "Mutations of endo-beta-N-acetylglucosaminidase H active site residue
RT Assp130 and Glu132: activities and conformations.";
RL Protein Sci. 8:2338-2346(1999).
CC -!- FUNCTION: Cleaves asparagine-linked oligomannose and hybrid, but not
CC complex, oligosaccharides from glycoproteins.
CC {ECO:0000269|PubMed:10595536, ECO:0000269|PubMed:7663942}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ProZyme product sheet;
CC URL="https://prozyme.com/products/gke-5002";
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DR EMBL; K02182; AAA26738.1; -; Genomic_DNA.
DR PIR; A00903; RBSMHP.
DR PDB; 1C3F; X-ray; 2.10 A; A=48-312.
DR PDB; 1C8X; X-ray; 2.00 A; A=48-312.
DR PDB; 1C8Y; X-ray; 2.00 A; A=48-312.
DR PDB; 1C90; X-ray; 2.10 A; A/B=48-312.
DR PDB; 1C91; X-ray; 2.10 A; A=48-312.
DR PDB; 1C92; X-ray; 2.10 A; A=48-312.
DR PDB; 1C93; X-ray; 2.10 A; A=48-312.
DR PDB; 1EDT; X-ray; 1.90 A; A=43-313.
DR PDB; 6VE1; X-ray; 2.10 A; A/B/C/D=47-313.
DR PDBsum; 1C3F; -.
DR PDBsum; 1C8X; -.
DR PDBsum; 1C8Y; -.
DR PDBsum; 1C90; -.
DR PDBsum; 1C91; -.
DR PDBsum; 1C92; -.
DR PDBsum; 1C93; -.
DR PDBsum; 1EDT; -.
DR PDBsum; 6VE1; -.
DR AlphaFoldDB; P04067; -.
DR SASBDB; P04067; -.
DR SMR; P04067; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR BRENDA; 3.2.1.96; 6076.
DR EvolutionaryTrace; P04067; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; 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; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..42
FT /note="Or 44"
FT /evidence="ECO:0000269|PubMed:6429133"
FT CHAIN 43..313
FT /note="Endo-beta-N-acetylglucosaminidase H"
FT /id="PRO_0000011958"
FT DOMAIN 51..307
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000305|PubMed:10595536"
FT MUTAGEN 172
FT /note="D->A,E: 2% activity."
FT /evidence="ECO:0000269|PubMed:10595536"
FT MUTAGEN 172
FT /note="D->N: 0.1% activity."
FT /evidence="ECO:0000269|PubMed:10595536"
FT MUTAGEN 174
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10595536"
FT MUTAGEN 174
FT /note="E->D,Q: 0.05% activity."
FT /evidence="ECO:0000269|PubMed:10595536"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1EDT"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1EDT"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:1EDT"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1C8X"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1C93"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1EDT"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1EDT"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:1EDT"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1EDT"
SQ SEQUENCE 313 AA; 33052 MW; 69E25DE1A615CF71 CRC64;
MFTPVRRRVR TAALALSAAA ALVLGSTAAS GASATPSPAP APAPAPVKQG PTSVAYVEVN
NNSMLNVGKY TLADGGGNAF DVAVIFAANI NYDTGTKTAY LHFNENVQRV LDNAVTQIRP
LQQQGIKVLL SVLGNHQGAG FANFPSQQAA SAFAKQLSDA VAKYGLDGVD FDDEYAEYGN
NGTAQPNDSS FVHLVTALRA NMPDKIISLY NIGPAASRLS YGGVDVSDKF DYAWNPYYGT
WQVPGIALPK AQLSPAAVEI GRTSRSTVAD LARRTVDEGY GVYLTYNLDG GDRTADVSAF
TRELYGSEAV RTP
