{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8A6W6","uniProtkbId":"GHLEV_BACTN","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-06-01","entryVersion":122,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)","taxonId":226186,"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Bacteroidaceae","Bacteroides"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28103254"}],"value":"Endo-levanase BT_1760"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20603004"}],"value":"Levanase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}],"value":"3.2.1.65"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20603004"}],"value":"Beta 2,6-specific endo-acting fructanase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20603004"}],"value":"Beta 2,6 endo-fructanase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"37286596"}],"value":"GH(lev)"}}],"flag":"Precursor"},"genes":[{"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAO76867.1"}],"value":"BT_1760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}],"value":"Part of a polysaccharide utilization locus (PUL) involved in the acquisition and degradation of levan, a natural polymer made up of fructose molecules connected by 2,6 beta glycosidic linkages (PubMed:20603004). Acts as a beta 2,6-specific endo-acting fructanase that cleaves the levan polymer (PubMed:20603004, PubMed:28103254). It degrades levans to fructo-oligosaccharides (FOS) with degree of polymerization from 2 to 13, providing a prebiotic substrate for gut microbiota (PubMed:28103254). It can use bacterial levans and levan of Timothy grass as substrates (PubMed:28103254). It cannot degrade beta 2,1 fructans, inulin-type FOS, dahlia inulin, xylooligosaccharides, raffinose and stachyose (PubMed:20603004, PubMed:28103254)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Random hydrolysis of (2->6)-beta-D-fructofuranosidic linkages in (2->6)-beta-D-fructans (levans) containing more than 3 fructose units.","ecNumber":"3.2.1.65","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.6,"unit":"mM","substrate":"levan","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}],"value":"kcat is 32987 min(-1) with levan as substrate (PubMed:20603004). kcat is 466 sec(-1) with levan synthesized by wild-type Lsc3 from sucrose as substrate (PubMed:28103254). kcat is 366 sec(-1) with levan synthesized by wild-type Lsc3 from raffinose as substrate (PubMed:28103254). kcat is 472 sec(-1) with levan synthesized by Lsc3 D300N mutant as substrate (PubMed:28103254). kcat is 442 sec(-1) with levan of Zymomonas mobilis as substrate (PubMed:28103254). kcat is 333 sec(-1) with levan of Halomonas smyrnensis as substrate (PubMed:28103254). kcat is 901 sec(-1) with levan of Timothy grass as substrate (PubMed:28103254)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}],"value":"Optimum pH is 5.5-6-0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28103254"}],"value":"Optimum temperature is 50 degrees Celsius, but incubation of the enzyme at 50 degrees Celsius for 30 minutes strongly decreases its activity (PubMed:28103254). It shows perfect stability and activity at 37 degrees Celsius, the internal temperature of the human body (PubMed:28103254)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37286596"}],"value":"The core SusCD(lev) complex, the surface glycan-binding protein BT_1761 (SGBP(lev)) and the endo-levanase BT_1760 (GH(lev)) form a stable four-component outer membrane levan utilisome complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31186460"}],"value":"Cell outer membrane","id":"SL-0040"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Lipid-anchor","id":"SL-9901"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31186460"}],"value":"Extracellular side","id":"SL-9911"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"}],"value":"Expressed early during growth on rich media (PubMed:20603004). Induced in the presence of fructose-containing carbohydrates (PubMed:20603004)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31186460"}],"value":"Contains a catalytic N-terminal five-bladed beta-propeller domain connected with a C-terminal beta-sandwich domain (PubMed:31186460). The C-terminal domain is probably needed for correct folding, solubility and stability of the whole protein (PubMed:31186460)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20603004"}],"value":"The deletion mutant does not grow on levan, but shows normal growth on all other media tested including beta 2,1-linked fructo-oligosaccharides, with doubling times comparable to wild-type on fructose, sucrose and fructo-oligosaccharides"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 32 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"Endo-levanase BT_1760","featureId":"PRO_5004303154"},{"type":"Active site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31186460"}]},{"type":"Active site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31186460"}]},{"type":"Lipidation","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Mutagenesis","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Loss of activity. 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