EBA1_ELIME
ID EBA1_ELIME Reviewed; 339 AA.
AC P36911;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Endo-beta-N-acetylglucosaminidase F1;
DE EC=3.2.1.96;
DE AltName: Full=Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1;
DE AltName: Full=Endoglycosidase F1;
DE AltName: Full=Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1;
DE Flags: Precursor;
GN Name=endOF1;
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 PROTEIN SEQUENCE OF 51-77; 108-161
RP AND 265-338.
RX PubMed=1740434; DOI=10.1016/s0021-9258(19)50606-8;
RA Tarentino A.L., Quinones G., Schrader W.P., Changchien L.-M.,
RA Plummer T.H. Jr.;
RT "Multiple endoglycosidase (Endo) F activities expressed by Flavobacterium
RT meningosepticum. Endo F1: molecular cloning, primary sequence, and
RT structural relationship to Endo H.";
RL J. Biol. Chem. 267:3868-3872(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7947807; DOI=10.1021/bi00251a005;
RA van Roey P., Rao V., Plummer T.H. Jr., Tarentino A.L.;
RT "Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-
RT barrel enzyme adapted for a complex substrate.";
RL Biochemistry 33:13989-13996(1994).
CC -!- FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins. Does not hydrolyze complex
CC bi- or triantennary glycans. The presence of a core-bound fucose
CC impedes endo F1 hydrolysis.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; M80793; AAA24922.1; -; Genomic_DNA.
DR PIR; A42259; A42259.
DR PDB; 2EBN; X-ray; 2.00 A; A=51-339.
DR PDBsum; 2EBN; -.
DR AlphaFoldDB; P36911; -.
DR SMR; P36911; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EvolutionaryTrace; P36911; -.
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; IPR016289; Endo-Fsp.
DR InterPro; IPR001223; Glyco_hydro18_cat.
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; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..50
FT /note="Or 51, or 52"
FT /evidence="ECO:0000269|PubMed:1740434"
FT CHAIN 51..338
FT /note="Endo-beta-N-acetylglucosaminidase F1"
FT /id="PRO_0000011954"
FT PROPEP 339
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000011955"
FT DOMAIN 60..326
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2EBN"
FT TURN 306..311
FT /evidence="ECO:0007829|PDB:2EBN"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:2EBN"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2EBN"
SQ SEQUENCE 339 AA; 37201 MW; 2EB8D798F9E8CF0A CRC64;
MKKFINQFSA SLKNNILVFL AFPFVWTSCA RDNPLSSENS NISPNAAARA AVTGTTKANI
KLFSFTEVND TNPLNNLNFT LKNSGKPLVD MVVLFSANIN YDAANDKVFV SNNPNVQHLL
TNRAKYLKPL QDKGIKVILS ILGNHDRSGI ANLSTARAKA FAQELKNTCD LYNLDGVFFD
DEYSAYQTPP PSGFVTPSNN AAARLAYETK QAMPNKLVTV YVYSRTSSFP TAVDGVNAGS
YVDYAIHDYG GSYDLATNYP GLAKSGMVMS SQEFNQGRYA TAQALRNIVT KGYGGHMIFA
MDPNRSNFTS GQLPALKLIA KELYGDELVY SNTPYSKDW
