INUS_LACGS
ID INUS_LACGS Reviewed; 761 AA.
AC D3WYV9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Inulosucrase {ECO:0000303|PubMed:20075040};
DE Short=IS {ECO:0000303|PubMed:23645191};
DE EC=2.4.1.9 {ECO:0000269|PubMed:20075040};
DE Flags: Precursor;
GN Name=inuGB {ECO:0000303|PubMed:20075040};
GN Synonyms=ftf {ECO:0000303|PubMed:20075040};
OS Lactobacillus gasseri.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1596;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=DSM 20604 / V 4020/4079;
RX PubMed=20075040; DOI=10.1099/mic.0.036616-0;
RA Anwar M.A., Kralj S., Pique A.V., Leemhuis H., van der Maarel M.J.,
RA Dijkhuizen L.;
RT "Inulin and levan synthesis by probiotic Lactobacillus gasseri strains:
RT characterization of three novel fructansucrase enzymes and their fructan
RT products.";
RL Microbiology 156:1264-1274(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 20604 / V 4020/4079;
RX PubMed=23645191; DOI=10.1128/aem.00854-13;
RA Diez-Municio M., de las Rivas B., Jimeno M.L., Munoz R., Moreno F.J.,
RA Herrero M.;
RT "Enzymatic synthesis and characterization of fructooligosaccharides and
RT novel maltosylfructosides by inulosucrase from Lactobacillus gasseri DSM
RT 20604.";
RL Appl. Environ. Microbiol. 79:4129-4140(2013).
CC -!- FUNCTION: Fructosyltransferase that catalyzes the polymerization of the
CC fructose moiety of sucrose to produce inulin polymer and a broad range
CC of inulin oligosaccharides ranging from DP2-DP13. Is also able to
CC convert raffinose into a fructan polymer and fructo-oligosaccharides
CC (FOS) in vitro; however, L.gasseri strain DSM 20604 is unable to
CC ferment raffinose. Can also transfer fructose moieties of sucrose to
CC maltose, leading to maltosylfructosides (MFOS). Also displays sucrose
CC hydrolase activity. {ECO:0000269|PubMed:20075040,
CC ECO:0000269|PubMed:23645191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2->1)-beta-D-fructosyl](n) + sucrose = [(2->1)-beta-D-
CC fructosyl](n+1) + D-glucose; Xref=Rhea:RHEA:15745, Rhea:RHEA-
CC COMP:10036, Rhea:RHEA-COMP:14296, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:17992, ChEBI:CHEBI:29084; EC=2.4.1.9;
CC Evidence={ECO:0000269|PubMed:20075040, ECO:0000269|PubMed:23645191};
CC -!- ACTIVITY REGULATION: Calcium ions are required for optimal activity,
CC but do not seem to be essential since addition of EDTA causes only a
CC 30% drop in activity. {ECO:0000269|PubMed:20075040}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5-4.5. {ECO:0000269|PubMed:20075040};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Activity drastically
CC decreases at 60 degrees Celsius. {ECO:0000269|PubMed:20075040};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20075040}. Cell
CC surface {ECO:0000269|PubMed:20075040}. Note=Lacks the cell-wall-
CC anchoring LPXTG/LPKAG motif found in protein orthologs, resulting in a
CC partly free and partly cell-associated subcellular location status.
CC {ECO:0000269|PubMed:20075040}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; GU166814; ACZ67286.1; -; Genomic_DNA.
DR AlphaFoldDB; D3WYV9; -.
DR SMR; D3WYV9; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR BRENDA; 2.4.1.9; 2868.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047725; F:inulosucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0050053; F:levansucrase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR CDD; cd08997; GH68; 1.
DR Gene3D; 2.115.10.20; -; 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; SSF75005; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Glycosyltransferase; Metal-binding;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..761
FT /note="Inulosucrase"
FT /id="PRO_0000431247"
FT REGION 54..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 518
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 418..419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 516..518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 419
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
SQ SEQUENCE 761 AA; 83277 MW; 129BEF6FBDD40082 CRC64;
MLENKNHKKM SLSGKSLLMG TLSTAAIVLS ASTVNAATTN ADNVTKNQTV AVSATTTNNE
TNNQVSSSSE KTADSKTEKD TNLTSAATKE VKADAAKTTS PVNNVKTVAD TTTTTKETTD
NTEKSPVNFS ADVKKNDAVK QDEKAATAVK ANTEVKANET STKSASKDNK AELKGQIKDI
VKESGVDTSK LTDDQINELN KISFSKEAKS GTQLTYSDFK KIAKTLIEQD ARYAVPFFNA
SKIKNMPAAK TLDAQTGKVE DLEIWDSWPV QDAKTGYVSN WNGYQLVIGM MGVPNTNDNH
IYLLYNKYGD NNFNNWKNAG PIFGLGTPVI QQWSGSATLN KDGSIQLYYT KVDTSDNNTN
HQKIASATVY LNLEKNQDKI SIAHVDNDHI VFEGDGYHYQ TYNQWKKTNK GADNIAMRDA
HVIDDKDGNR YLVFEASTGT ENYQGADQIY QWLNYGGTNK DNLGDFLQIL SNSDIKDRAK
WSNAAIGIIK LNNDTKNPGV EKVYTPLISA PMVSDEIERP DVVRLGNKYY LFAATRLNRG
SNDDAWMAAN KAVGDNVAMI GYVSDNLTHG YVPLNESGVV LTASVPANWR TATYSYYAVP
VEGRDDQLLI TSYITNRGEV AGKGMHATWA PSFLLQINPD NTTTVLAKMT NQGDWIWDDS
SENADMMGVL EKDAPNSAAL PGEWGKPVDW DLIGGYNLKP HQPVTPIPNV PTTPEKPENP
TTPNTPDTPH TPTTPNTPDT PRTPEVPTTP VKKTTQSELR S
