EBI1_BIFLS
ID EBI1_BIFLS Reviewed; 545 AA.
AC B7GPC7; E8MPN7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Endo-beta-N-acetylglucosaminidase {ECO:0000303|PubMed:22745059};
DE EC=3.2.1.96 {ECO:0000269|PubMed:22745059};
DE AltName: Full=Endoglycosidase BI-1 {ECO:0000303|PubMed:22745059};
DE Short=EndoBI-1 {ECO:0000303|PubMed:22745059};
DE Flags: Precursor;
GN OrderedLocusNames=Blon_2468 {ECO:0000312|EMBL:ACJ53522.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, MUTAGENESIS OF GLU-184, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=22745059; DOI=10.1074/mcp.m112.018119;
RA Garrido D., Nwosu C., Ruiz-Moyano S., Aldredge D., German J.B.,
RA Lebrilla C.B., Mills D.A.;
RT "Endo-beta-N-acetylglucosaminidases from infant gut-associated
RT bifidobacteria release complex N-glycans from human milk glycoproteins.";
RL Mol. Cell. Proteomics 11:775-785(2012).
CC -!- FUNCTION: Endoglycosidase with broad specificity that cleaves the
CC chitobiose core of high mannose and complex N-linked glycans. Is able
CC to release N-glycans from diverse host glycoproteins such as human and
CC bovine lactoferrin, immunoglobulins A and G, and ribonuclease B. Is
CC active directly on human breast milk - a complex matrix of lipids,
CC oligosaccharides, and proteins with disparate glycosylation types
CC - successfully removing a significant proportion of the total amount of
CC N-glycans. Does not recognize O-linked glycans or free human milk
CC oligosaccharides (HMO). {ECO:0000269|PubMed:22745059}.
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 Evidence={ECO:0000269|PubMed:22745059};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:22745059};
CC Temperature dependence:
CC Optimum temperature is 30-45 degrees Celsius. Is heat-resistant,
CC since the enzymatic activity is not significantly impaired by
CC incubation at 95 degrees Celsius for 1 or 5 minutes.
CC {ECO:0000269|PubMed:22745059};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed. Is up-regulated when cells are
CC grown on lactose (by comparison with cells grown on glucose), or when
CC the bacterium is incubated with human or bovine lactoferrin.
CC {ECO:0000269|PubMed:22745059}.
CC -!- BIOTECHNOLOGY: EndoBI-1 might prove useful as a novel tool for diverse
CC applications in proteomics and glycoproteomics research.
CC {ECO:0000305|PubMed:22745059}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; CP001095; ACJ53522.1; -; Genomic_DNA.
DR RefSeq; WP_012578681.1; NZ_JDTT01000013.1.
DR AlphaFoldDB; B7GPC7; -.
DR SMR; B7GPC7; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; B7GPC7; -.
DR EnsemblBacteria; ACJ53522; ACJ53522; Blon_2468.
DR KEGG; bln:Blon_2468; -.
DR PATRIC; fig|391904.8.peg.2542; -.
DR OMA; WISMYDI; -.
DR BRENDA; 3.2.1.96; 849.
DR Proteomes; UP000001360; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035977; P:protein deglycosylation involved in glycoprotein catabolic process; IDA:UniProtKB.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..545
FT /note="Endo-beta-N-acetylglucosaminidase"
FT /id="PRO_5000417322"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..333
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 486..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT MUTAGEN 184
FT /note="E->N: Loss of enzymatic activity. Binds to the core
FT of N-glycans, Man(3)GlcNAc(2). Also shows significant
FT binding to the alpha1-6-fucosylated pentasaccharide,
FT characteristic of human N-linked glycoproteins."
FT /evidence="ECO:0000269|PubMed:22745059"
SQ SEQUENCE 545 AA; 59826 MW; 9DA332EF43362C80 CRC64;
MTFIKQMMPR YVASMTAGIV AAAMAATCAF APVANADAVS PTQETIQSTG RHFMVYYRAW
RDVTMKGVNT DLPDDNWISM YDIPYGVDVV NIFSYVPSGQ EEQAQPFYDK LKSDYAPYLH
SRGIKLVRGI DYTGVAVNGF RTFMKEQNKT ESEATEADYD AYAKQVIDKY MISVGLDGLD
IDMEAHPNDA DVKISDNVIR ALSKHIGPKS AKPDTTMFLY DTNGSYLNPF KNVAECFDYV
AYQQYGSSSD RTARAAADYQ PYIGNEFVPG LTFPEEGDMN NRWYDATEPY EESHFYQVAS
YVREHNLGGM FVYALDRDGR NYDEDLRRIV PSNLLWTKTA IAESEGMALD TAKTAANHYL
DRMSLRQVID DNAASADKAR DMVGKAANLY ETNKAVLGGD YGEGFSNTYD PTLEAGLLGI
DISVLQQQID KSSEIIGADT AESDAKTALR MARDAAIDGL TGKIYTADQV SAWSQALKAA
LDATVPVPTP DSTDQNGNRD KVTNHKVQGQ PKQLSATGIS TDIIVAVGVT LAIAGVALSL
SRKLS
