ID A0A0B0D7L4_9BACI Unreviewed; 437 AA.
AC A0A0B0D7L4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 05-FEB-2025, entry version 24.
DE SubName: Full=Levansucrase {ECO:0000313|EMBL:KHE71094.1};
GN ORFNames=LD39_10560 {ECO:0000313|EMBL:KHE71094.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE71094.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE71094.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE71094.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR603469-3};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family.
CC {ECO:0000256|ARBA:ARBA00006775, ECO:0000256|RuleBase:RU361220}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHE71094.1}.
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DR EMBL; JRNX01000332; KHE71094.1; -; Genomic_DNA.
DR RefSeq; WP_035546060.1; NZ_JRNX01000332.1.
DR AlphaFoldDB; A0A0B0D7L4; -.
DR OrthoDB; 2210426at2; -.
DR Proteomes; UP000030879; Unassembled WGS sequence.
DR GO; GO:0050053; F:levansucrase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR CDD; cd08997; GH68; 1.
DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 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 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR603469-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603469-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039056931"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-1"
FT ACT_SITE 314
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-1"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-2"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-2"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-3"
FT BINDING 312..314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-2"
FT SITE 230
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR603469-4"
SQ SEQUENCE 437 AA; 48593 MW; C7BC9C2EF5DC62A1 CRC64;
MKRGKRLSVV QGVALSAIML VGGLVQAPGI VSAAEQNETE TAVWSREDAQ NYNLSENNTA
PNIDNVDEVA PDYWVWDTWP LRNRDGSIAT VNGYKVVFAL TASKDYTWSG RHDHAAIRYF
YSKNGKDWEM GGLAYDQEKA LGSRQWAGSA MMEEDGKVHL FYTASGRKGE ETTTFEQRLA
KTTFDIGVDK KNKSIELSNF GEHMILAEAD GEYYETQDQK TGNIIYSFRD PWFFQDPKTE
KEYIIFEGNS AGYEKTLDPE NIGSEEFREN HEVPAGAEDY NGNIGIASAE NGDLTEFELL
PPLLEADGVN QQLERPHVLV KGGQYYLFTI SHQFTFAPGL NGPDGLYGFV NESLRGDYEP
LNDNGLVLAN PENDPFMTYS HAVMPNGTVI SFVNEYIDEN GDRQLGGTFA PTLKLSIHGD
ETKVNGTLKA GQIIPSH
//