ID LSC_BACSU Reviewed; 473 AA. AC P05655; P70984; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Levansucrase {ECO:0000303|PubMed:4206083}; DE EC=2.4.1.10 {ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628, ECO:0000269|PubMed:4206083}; DE AltName: Full=Beta-D-fructofuranosyl transferase {ECO:0000303|PubMed:6424671}; DE AltName: Full=Fructosyltransferase {ECO:0000303|PubMed:14517548}; DE Short=FTF {ECO:0000303|PubMed:14517548}; DE AltName: Full=Sucrose 6-fructosyl transferase; DE Flags: Precursor; GN Name=sacB {ECO:0000303|PubMed:6424671}; OrderedLocusNames=BSU34450; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC STRAIN=168; RX PubMed=2993818; DOI=10.1007/bf00425427; RA Steinmetz M., Le Coq D., Aymerich S., Gonzy-Treboul G., Gay P.; RT "The DNA sequence of the gene for the secreted Bacillus subtilis enzyme RT levansucrase and its genetic control sites."; RL Mol. Gen. Genet. 200:220-228(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Denizot F.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. RC STRAIN=168 / PY79; RX PubMed=6424671; DOI=10.1016/s0006-291x(84)80320-4; RA Fouet A., Arnaud M., Klier A., Rapoport G.; RT "Characterization of the precursor form of the exocellular levansucrase RT from Bacillus subtilis."; RL Biochem. Biophys. Res. Commun. 119:795-800(1984). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68, AND INDUCTION. RX PubMed=2428811; DOI=10.1128/jb.168.1.380-388.1986; RA Shimotsu H., Henner D.J.; RT "Modulation of Bacillus subtilis levansucrase gene expression by sucrose RT and regulation of the steady-state mRNA level by sacU and sacQ genes."; RL J. Bacteriol. 168:380-388(1986). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=4206083; DOI=10.1111/j.1432-1033.1974.tb03269.x; RA Chambert R., Treboul G., Dedonder R.; RT "Kinetic studies of levansucrase of Bacillus subtilis."; RL Eur. J. Biochem. 41:285-300(1974). RN [7] RP SUBUNIT, AND AMINO ACID COMPOSITION. RX PubMed=807261; DOI=10.1016/s0300-9084(75)80105-2; RA Gonzy-Treboul G., Chambert R., Dedonder R.; RT "Levansucrase of Bacillus subtilis: reexamination of some physical and RT chemical properties."; RL Biochimie 57:17-28(1975). RN [8] RP INDUCTION. RX PubMed=11739774; DOI=10.1099/00221287-147-12-3413; RA Pereira Y., Petit-Glatron M.-F., Chambert R.; RT "yveB, encoding endolevanase LevB, is part of the sacB-yveB-yveA RT levansucrase tricistronic operon in Bacillus subtilis."; RL Microbiology 147:3413-3419(2001). RN [9] RP ACTIVITY REGULATION. RC STRAIN=168; RX PubMed=26256357; DOI=10.1016/j.carbpol.2015.06.056; RA Porras-Dominguez J.R., Avila-Fernandez A., Miranda-Molina A., RA Rodriguez-Alegria M.E., Munguia A.L.; RT "Bacillus subtilis 168 levansucrase (SacB) activity affects average levan RT molecular weight."; RL Carbohydr. Polym. 132:338-344(2015). RN [10] {ECO:0007744|PDB:1OYG, ECO:0007744|PDB:1PT2} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 30-473 IN COMPLEX WITH CA(2+) AND RP OF MUTANT ALA-342 IN COMPLEX WITH CA(2+) AND SUCROSE, FUNCTION, CATALYTIC RP ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, AND MUTAGENESIS OF ASP-86; RP ASP-247 AND GLU-342. RX PubMed=14517548; DOI=10.1038/nsb974; RA Meng G., Futterer K.; RT "Structural framework of fructosyl transfer in Bacillus subtilis RT levansucrase."; RL Nat. Struct. Biol. 10:935-941(2003). RN [11] {ECO:0007744|PDB:2VDT} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 34-472 OF MUTANT ALA-164 IN RP COMPLEX WITH CA(2+), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF SER-164; HIS-243; ILE-341; ALA-344; ARG-360; RP GLY-361; PHE-414; TYR-429 AND ARG-433. RX PubMed=18596022; DOI=10.1093/protein/gzn036; RA Ortiz-Soto M.E., Rivera M., Rudino-Pinera E., Olvera C., Lopez-Munguia A.; RT "Selected mutations in Bacillus subtilis levansucrase semi-conserved RT regions affecting its biochemical properties."; RL Protein Eng. Des. Sel. 21:589-595(2008). RN [12] {ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, ECO:0007744|PDB:3BYL, ECO:0007744|PDB:3BYN} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS ALA-86; ALA-247 AND RP ALA-342 IN COMPLEXES WITH CA(2+) AND RAFFINOSE. RA Meng G., Futterer K.; RT "Donor substrate recognition in the raffinose-bound E342A mutant of RT fructosyltransferase Bacillus subtilis levansucrase."; RL Submitted (JAN-2008) to the PDB data bank. RN [13] {ECO:0007744|PDB:6PWQ} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 30-473 OF MUTANT ALA-164 IN RP COMPLEX WITH CA(2+), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF SER-164. RX PubMed=32553967; DOI=10.1016/j.ijbiomac.2020.06.114; RA Ortiz-Soto M.E., Porras-Dominguez J.R., Rodriguez-Alegria M.E., RA Morales-Moreno L.A., Diaz-Vilchis A., Rudino-Pinera E., RA Beltran-Hernandez N.E., Rivera H.M., Seibel J., Lopez Munguia A.; RT "Implications of the mutation S164A on Bacillus subtilis levansucrase RT product specificity and insights into protein interactions acting upon RT levan synthesis."; RL Int. J. Biol. Macromol. 161:898-908(2020). RN [14] {ECO:0007744|PDB:6VHQ} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 30-473 OF MUTANT ALA-86/ALA-342 RP IN COMPLEX WITH CA(2+) AND LEVAN-TYPE HEXASACCHARIDES, FUNCTION, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-117; RP PHE-182; TYR-187; TYR-237; ASN-242 AND LYS-363. RX PubMed=33303628; DOI=10.1074/jbc.ra120.015853; RA Raga-Carbajal E., Diaz-Vilchis A., Rojas-Trejo S.P., Rudino-Pinera E., RA Olvera C.; RT "The molecular basis of the nonprocessive elongation mechanism in RT levansucrases."; RL J. Biol. Chem. 296:100178-100178(2021). CC -!- FUNCTION: Catalyzes the synthesis of levan, a fructose polymer, by CC transferring the fructosyl moiety from sucrose to a growing acceptor CC molecule (PubMed:4206083, PubMed:14517548, PubMed:18596022, CC PubMed:32553967, PubMed:33303628). Also displays sucrose hydrolase CC activity (PubMed:4206083, PubMed:18596022, PubMed:32553967, CC PubMed:33303628). At low sucrose concentrations, functions as an CC hydrolase with water as acceptor, whereas at higher substrate CC concentrations it adds fructosyl units to a growing levan chain CC (PubMed:4206083). {ECO:0000269|PubMed:14517548, CC ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, CC ECO:0000269|PubMed:33303628, ECO:0000269|PubMed:4206083}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + CC sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D- CC glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA- CC COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, CC ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; CC Evidence={ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:18596022, CC ECO:0000269|PubMed:32553967, ECO:0000269|PubMed:33303628, CC ECO:0000269|PubMed:4206083}; CC -!- ACTIVITY REGULATION: Ca(2+) may play an important structural role and CC promote stability of levansucrase (PubMed:14517548). The enzyme CC concentration is a factor defining the molecular weight (MW) levan CC distribution (PubMed:26256357). A bimodal distribution is reported at CC the usual enzyme concentrations (PubMed:26256357). At low CC concentrations, the enzyme synthesizes high MW levan, and at high CC concentrations, it synthesizes low MW levan (PubMed:26256357). CC {ECO:0000269|PubMed:14517548, ECO:0000269|PubMed:26256357}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8 mM for sucrose {ECO:0000269|PubMed:18596022}; CC KM=9 mM for sucrose {ECO:0000269|PubMed:33303628}; CC KM=8.3 mM for sucrose (for hydrolysis, in the absence of levan F4) CC {ECO:0000269|PubMed:32553967}; CC KM=6.9 mM for sucrose (for hydrolysis, in the presence of 5 g/L levan CC F4) {ECO:0000269|PubMed:32553967}; CC KM=6.8 mM for sucrose (for hydrolysis, in the presence of 55 g/L CC levan F4) {ECO:0000269|PubMed:32553967}; CC KM=57.6 mM for sucrose (for transfructosylation, in the absence of CC levan F4) {ECO:0000269|PubMed:32553967}; CC KM=20.9 mM for sucrose (for transfructosylation, in the presence of 5 CC g/L levan F4) {ECO:0000269|PubMed:32553967}; CC KM=10.9 mM for sucrose (for transfructosylation, in the presence of CC 55 g/L levan F4) {ECO:0000269|PubMed:32553967}; CC Note=kcat is 164.6 sec(-1) with sucrose as substrate CC (PubMed:18596022). kcat is 236.7 sec(-1) with sucrose as substrate CC (PubMed:33303628). kcat is 71.2 sec(-1) with sucrose as substrate CC (for hydrolysis, in the absence of levan F4). kcat is 69.8 sec(-1) CC with sucrose as substrate (for hydrolysis, in the presence of 5 g/L CC levan F4). kcat is 65.9 sec(-1) with sucrose as substrate (for CC hydrolysis, in the presence of 55 g/L levan F4). kcat is 26.6 sec(-1) CC with sucrose as substrate (for transfructosylation, in the absence of CC levan F4). kcat is 33.0 sec(-1) with sucrose as substrate (for CC transfructosylation, in the presence of 5 g/L levan F4). kcat is 33.7 CC sec(-1) with sucrose as substrate (for transfructosylation, in the CC presence of 55 g/L levan F4) (PubMed:32553967). CC {ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, CC ECO:0000269|PubMed:33303628}; CC pH dependence: CC Optimum pH is 6. {ECO:0000269|PubMed:18596022}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:807261}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- INDUCTION: Induced by sucrose (PubMed:2428811, PubMed:11739774). CC Expression is controlled by the sacR non-coding regulatory region, CC located upstream from sacB (PubMed:2993818, PubMed:2428811). CC {ECO:0000269|PubMed:11739774, ECO:0000269|PubMed:2428811, CC ECO:0000269|PubMed:2993818}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14202; AAA22725.1; -; Genomic_DNA. DR EMBL; Z94043; CAB08015.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15450.1; -; Genomic_DNA. DR EMBL; K01987; AAA22724.1; -; Genomic_DNA. DR EMBL; X02730; CAA26513.1; -; Genomic_DNA. DR PIR; S07309; A25040. DR RefSeq; NP_391325.1; NC_000964.3. DR RefSeq; WP_001022105.1; NZ_JNCM01000033.1. DR PDB; 1OYG; X-ray; 1.50 A; A=30-473. DR PDB; 1PT2; X-ray; 2.10 A; A=30-473. DR PDB; 2VDT; X-ray; 3.20 A; A=34-472. DR PDB; 3BYJ; X-ray; 2.10 A; A=1-473. DR PDB; 3BYK; X-ray; 2.10 A; A=1-473. DR PDB; 3BYL; X-ray; 2.10 A; A=1-473. DR PDB; 3BYN; X-ray; 2.10 A; A=1-473. DR PDB; 6PWQ; X-ray; 2.60 A; A/B=30-473. DR PDB; 6VHQ; X-ray; 2.05 A; A/B=30-473. DR PDBsum; 1OYG; -. DR PDBsum; 1PT2; -. DR PDBsum; 2VDT; -. DR PDBsum; 3BYJ; -. DR PDBsum; 3BYK; -. DR PDBsum; 3BYL; -. DR PDBsum; 3BYN; -. DR PDBsum; 6PWQ; -. DR PDBsum; 6VHQ; -. DR AlphaFoldDB; P05655; -. DR SMR; P05655; -. DR STRING; 224308.BSU34450; -. DR DrugBank; DB02772; Sucrose. DR CAZy; GH68; Glycoside Hydrolase Family 68. DR PaxDb; 224308-BSU34450; -. DR EnsemblBacteria; CAB15450; CAB15450; BSU_34450. DR GeneID; 936413; -. DR KEGG; bsu:BSU34450; -. DR PATRIC; fig|224308.179.peg.3732; -. DR eggNOG; COG1621; Bacteria. DR InParanoid; P05655; -. DR OrthoDB; 2210426at2; -. DR PhylomeDB; P05655; -. DR BioCyc; BSUB:BSU34450-MONOMER; -. DR BioCyc; MetaCyc:BSU34450-MONOMER; -. DR BRENDA; 2.4.1.10; 658. DR SABIO-RK; P05655; -. DR EvolutionaryTrace; P05655; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC. DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro. DR CDD; cd08997; GH68; 1. DR InterPro; IPR003469; Glyco_hydro_68. DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf. DR Pfam; PF02435; Glyco_hydro_68; 1. DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Glycosyltransferase; KW Metal-binding; Reference proteome; Secreted; Signal; Transferase. FT SIGNAL 1..29 FT /evidence="ECO:0000305|PubMed:6424671" FT CHAIN 30..473 FT /note="Levansucrase" FT /id="PRO_0000012249" FT ACT_SITE 86 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:14517548" FT ACT_SITE 342 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:14517548" FT BINDING 85 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 86 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 164 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 241 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, FT ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, FT ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, FT ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, FT ECO:0007744|PDB:6VHQ" FT BINDING 246 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 247 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 272 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, FT ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, FT ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, FT ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, FT ECO:0007744|PDB:6VHQ" FT BINDING 308 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, FT ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, FT ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, FT ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, FT ECO:0007744|PDB:6VHQ" FT BINDING 310 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, FT ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, FT ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, FT ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, FT ECO:0007744|PDB:6VHQ" FT BINDING 339 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0000269|PubMed:18596022, ECO:0000269|PubMed:32553967, FT ECO:0000269|PubMed:33303628, ECO:0007744|PDB:1OYG, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:2VDT, FT ECO:0007744|PDB:3BYJ, ECO:0007744|PDB:3BYK, FT ECO:0007744|PDB:3BYN, ECO:0007744|PDB:6PWQ, FT ECO:0007744|PDB:6VHQ" FT BINDING 340 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT BINDING 360 FT /ligand="sucrose" FT /ligand_id="ChEBI:CHEBI:17992" FT /evidence="ECO:0000269|PubMed:14517548, FT ECO:0007744|PDB:1PT2, ECO:0007744|PDB:3BYN" FT SITE 247 FT /note="Transition state stabilizer" FT /evidence="ECO:0000305|PubMed:14517548" FT MUTAGEN 86 FT /note="D->A: Lack of levan synthesis." FT /evidence="ECO:0000269|PubMed:14517548" FT MUTAGEN 117 FT /note="D->A: 2-fold decrease in catalytic efficiency. FT Synthesizes a bimodal levan molecular weight distribution." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 164 FT /note="S->A: Drastic decrease in catalytic efficiency. FT Slight increase in affinity for sucrose. Increases FT transfructosylation activity. Uses acceptors such as FT glucose and short levans with an average molecular weight FT of 7.6 kDa more efficiently than wild-type enzyme, leading FT to the enhanced synthesis of medium and high molecular FT weight polymer." FT /evidence="ECO:0000269|PubMed:18596022, FT ECO:0000269|PubMed:32553967" FT MUTAGEN 164 FT /note="S->K: Loss of activity." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 182 FT /note="F->A: 3.7-fold decrease in catalytic efficiency. FT 1.6-fold increase in KM for sucrose. Synthesizes only high FT molecular weight levans." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 182 FT /note="F->W: 2.1-fold decrease in catalytic efficiency. FT Synthesizes a bimodal levan molecular weight distribution." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 182 FT /note="F->Y: 1.7-fold decrease in catalytic efficiency. FT Synthesizes a bimodal levan molecular weight distribution." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 187 FT /note="Y->A: Slight decrease in catalytic efficiency. FT Synthesizes a bimodal levan molecular weight distribution." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 237 FT /note="Y->A: Slight decrease in catalytic efficiency. FT Synthesizes only high molecular weight levans." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 242 FT /note="N->A: 14.6-fold decrease in catalytic efficiency. FT 2.2-fold increase in KM for sucrose. Levans are barely FT formed." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 243 FT /note="H->L: Decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 247 FT /note="D->A: Lack of levan synthesis." FT /evidence="ECO:0000269|PubMed:14517548" FT MUTAGEN 341 FT /note="I->V: Increases transfructosylation activity." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 342 FT /note="E->A: Lack of levan synthesis." FT /evidence="ECO:0000269|PubMed:14517548" FT MUTAGEN 344 FT /note="A->P: Increases transfructosylation activity." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 360 FT /note="R->K: Decrease in catalytic efficiency. Reduces FT affinity for sucrose. Synthesizes mainly oligosaccharides, FT but can still catalyze the synthesis of low amounts of FT levan." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 360 FT /note="R->S: Drastic decrease in catalytic efficiency. FT Reduces affinity for sucrose. Synthesizes only FT oligosaccharides." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 361 FT /note="G->F: Drastic decrease in catalytic efficiency. FT Reduces affinity for sucrose. Synthesizes mainly FT oligosaccharides, but can still catalyze the synthesis of FT low amounts of levan." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 363 FT /note="K->A: 2.9-fold decrease in catalytic efficiency. FT Synthesizes only high molecular weight levans." FT /evidence="ECO:0000269|PubMed:33303628" FT MUTAGEN 414 FT /note="F->W: Increases transfructosylation activity." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 429 FT /note="Y->N: Drastic decrease in catalytic efficiency. FT Reduces affinity for sucrose. Synthesizes only FT oligosaccharides." FT /evidence="ECO:0000269|PubMed:18596022" FT MUTAGEN 433 FT /note="R->A: Drastic decrease in catalytic efficiency. FT Reduces affinity for sucrose. Synthesizes only FT oligosaccharides." FT /evidence="ECO:0000269|PubMed:18596022" FT CONFLICT 12 FT /note="V -> I (in Ref. 4; AAA22724)" FT /evidence="ECO:0000305" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 48..52 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 103..111 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 120..127 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 161..169 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 175..183 FT /evidence="ECO:0007829|PDB:1OYG" FT TURN 184..188 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 189..201 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 206..218 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 228..234 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 256..265 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:6PWQ" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 287..299 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 303..308 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 322..333 FT /evidence="ECO:0007829|PDB:1OYG" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 342..349 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 352..360 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 374..383 FT /evidence="ECO:0007829|PDB:1OYG" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 395..400 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:2VDT" FT STRAND 410..416 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 419..431 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 435..438 FT /evidence="ECO:0007829|PDB:2VDT" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:6VHQ" FT STRAND 447..452 FT /evidence="ECO:0007829|PDB:1OYG" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:1OYG" SQ SEQUENCE 473 AA; 52971 MW; 3FBF2F571B41D5B0 CRC64; MNIKKFAKQA TVLTFTTALL AGGATQAFAK ETNQKPYKET YGISHITRHD MLQIPEQQKN EKYQVPEFDS STIKNISSAK GLDVWDSWPL QNADGTVANY HGYHIVFALA GDPKNADDTS IYMFYQKVGE TSIDSWKNAG RVFKDSDKFD ANDSILKDQT QEWSGSATFT SDGKIRLFYT DFSGKHYGKQ TLTTAQVNVS ASDSSLNING VEDYKSIFDG DGKTYQNVQQ FIDEGNYSSG DNHTLRDPHY VEDKGHKYLV FEANTGTEDG YQGEESLFNK AYYGKSTSFF RQESQKLLQS DKKRTAELAN GALGMIELND DYTLKKVMKP LIASNTVTDE IERANVFKMN GKWYLFTDSR GSKMTIDGIT SNDIYMLGYV SNSLTGPYKP LNKTGLVLKM DLDPNDVTFT YSHFAVPQAK GNNVVITSYM TNRGFYADKQ STFAPSFLLN IKGKKTSVVK DSILEQGQLT VNK //