{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B7GPC7","secondaryAccessions":["E8MPN7"],"uniProtkbId":"EBI1_BIFLS","entryAudit":{"firstPublicDate":"2015-06-24","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-02-10","entryVersion":89,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)","taxonId":391904,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Bifidobacteriales","Bifidobacteriaceae","Bifidobacterium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22745059"}],"value":"Endo-beta-N-acetylglucosaminidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}],"value":"3.2.1.96"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22745059"}],"value":"Endoglycosidase BI-1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22745059"}],"value":"EndoBI-1"}]}],"flag":"Precursor"},"genes":[{"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ACJ53522.1"}],"value":"Blon_2468"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}],"value":"Endoglycosidase with broad specificity that cleaves the chitobiose core of high mannose and complex N-linked glycans. Is able to release N-glycans from diverse host glycoproteins such as human and bovine lactoferrin, immunoglobulins A and G, and ribonuclease B. Is active directly on human breast milk - a complex matrix of lipids, oligosaccharides, and proteins with disparate glycosylation types - successfully removing a significant proportion of the total amount of N-glycans. Does not recognize O-linked glycans or free human milk oligosaccharides (HMO)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:73067"},{"database":"Rhea","id":"RHEA-COMP:12603"},{"database":"Rhea","id":"RHEA-COMP:18176"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:132248"},{"database":"ChEBI","id":"CHEBI:192714"},{"database":"ChEBI","id":"CHEBI:192715"}],"ecNumber":"3.2.1.96","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}],"value":"Optimum pH is 5.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}],"value":"Optimum temperature is 30-45 degrees Celsius. Is heat-resistant, since the enzymatic activity is not significantly impaired by incubation at 95 degrees Celsius for 1 or 5 minutes."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22745059"}],"value":"Constitutively expressed. Is up-regulated when cells are grown on lactose (by comparison with cells grown on glucose), or when the bacterium is incubated with human or bovine lactoferrin"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22745059"}],"value":"EndoBI-1 might prove useful as a novel tool for diverse applications in proteomics and glycoproteomics research"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 18 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"Endo-beta-N-acetylglucosaminidase","featureId":"PRO_5000417322"},{"type":"Transmembrane","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Domain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"GH18","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01258"}]},{"type":"Region","location":{"start":{"value":486,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01258"}]},{"type":"Mutagenesis","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Loss of enzymatic activity. Binds to the core of N-glycans, Man(3)GlcNAc(2). 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Natl. Acad. Sci. U.S.A.","firstPage":"18964","lastPage":"18969","volume":"105"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"22745059","citationType":"journal article","authors":["Garrido D.","Nwosu C.","Ruiz-Moyano S.","Aldredge D.","German J.B.","Lebrilla C.B.","Mills D.A."],"citationCrossReferences":[{"database":"PubMed","id":"22745059"},{"database":"DOI","id":"10.1074/mcp.m112.018119"}],"title":"Endo-beta-N-acetylglucosaminidases from infant gut-associated bifidobacteria release complex N-glycans from human milk glycoproteins.","publicationDate":"2012","journal":"Mol. Cell. Proteomics","firstPage":"775","lastPage":"785","volume":"11"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","INDUCTION","MUTAGENESIS OF GLU-184","BIOTECHNOLOGY"],"referenceComments":[{"value":"ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP001095","properties":[{"key":"ProteinId","value":"ACJ53522.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_012578681.1","properties":[{"key":"NucleotideSequenceId","value":"NC_011593.1"}]},{"database":"AlphaFoldDB","id":"B7GPC7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"B7GPC7","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH18","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 18"}]},{"database":"KEGG","id":"bln:Blon_2468","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"blon:BLIJ_2539","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|391904.8.peg.2542","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"BRENDA","id":"3.2.1.96","properties":[{"key":"OrganismId","value":"849"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0033925","properties":[{"key":"GoTerm","value":"F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22745059"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035977","properties":[{"key":"GoTerm","value":"P:protein deglycosylation involved in glycoprotein catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22745059"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR057677","properties":[{"key":"EntryName","value":"EndoE-GH18L_3HB-2"}]},{"database":"InterPro","id":"IPR057016","properties":[{"key":"EntryName","value":"EndoS_F2-like_TIM-barrel"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR001223","properties":[{"key":"EntryName","value":"Glyco_hydro18_cat"}]},{"database":"InterPro","id":"IPR001579","properties":[{"key":"EntryName","value":"Glyco_hydro_18_chit_AS"}]},{"database":"NCBIfam","id":"NF049901","properties":[{"key":"EntryName","value":"EndglycodaseB1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25528","properties":[{"key":"EntryName","value":"DUF7917"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23916","properties":[{"key":"EntryName","value":"TIM-barrel_EndoS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01095","properties":[{"key":"EntryName","value":"GH18_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51910","properties":[{"key":"EntryName","value":"GH18_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTFIKQMMPRYVASMTAGIVAAAMAATCAFAPVANADAVSPTQETIQSTGRHFMVYYRAWRDVTMKGVNTDLPDDNWISMYDIPYGVDVVNIFSYVPSGQEEQAQPFYDKLKSDYAPYLHSRGIKLVRGIDYTGVAVNGFRTFMKEQNKTESEATEADYDAYAKQVIDKYMISVGLDGLDIDMEAHPNDADVKISDNVIRALSKHIGPKSAKPDTTMFLYDTNGSYLNPFKNVAECFDYVAYQQYGSSSDRTARAAADYQPYIGNEFVPGLTFPEEGDMNNRWYDATEPYEESHFYQVASYVREHNLGGMFVYALDRDGRNYDEDLRRIVPSNLLWTKTAIAESEGMALDTAKTAANHYLDRMSLRQVIDDNAASADKARDMVGKAANLYETNKAVLGGDYGEGFSNTYDPTLEAGLLGIDISVLQQQIDKSSEIIGADTAESDAKTALRMARDAAIDGLTGKIYTADQVSAWSQALKAALDATVPVPTPDSTDQNGNRDKVTNHKVQGQPKQLSATGISTDIIVAVGVTLAIAGVALSLSRKLS","length":545,"molWeight":59826,"crc64":"9DA332EF43362C80","md5":"D235D1B2625FB0B054214DBFDDEB77BF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Domain":1,"Region":1,"Active site":1,"Mutagenesis":1},"uniParcId":"UPI000185BD26"}}