SACB_ERWAM
ID SACB_ERWAM Reviewed; 415 AA.
AC Q46654;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Levansucrase;
DE EC=2.4.1.10;
DE AltName: Full=Beta-D-fructofuranosyl transferase;
DE AltName: Full=Sucrose 6-fructosyl transferase;
GN Name=lsc;
OS Erwinia amylovora (Fire blight bacteria).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=552;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EA7/74;
RX AGRICOLA=IND20389464; DOI=10.1006/pmpp.1993.1029;
RA Geier G., Geider K.K.;
RT "Characterization and influence on virulence of the levansucrase gene from
RT the fireblight pathogen Erwinia amylovora.";
RL Physiol. Mol. Plant Pathol. 42:387-404(1993).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; X75079; CAA52972.1; -; Genomic_DNA.
DR PIR; S39195; S39195.
DR AlphaFoldDB; Q46654; -.
DR SMR; Q46654; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR BRENDA; 2.4.1.10; 2136.
DR PHI-base; PHI:2472; -.
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 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 3: Inferred from homology;
KW Glycosyltransferase; Secreted; Transferase.
FT CHAIN 1..415
FT /note="Levansucrase"
FT /id="PRO_0000057717"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 287
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 203
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
SQ SEQUENCE 415 AA; 46408 MW; 4FF564F6E0607FEB CRC64;
MSDYNYKPTL WTRADALKVH EDDPTTTQPV IDIAFPVMSE EVFIWDTMPL RDFDGEIISV
NGWCIIFTLT ADRNTDNPQF QDENGNYDIT RDWEDRHGRA RICYWYSRTG KDWIFGGRVM
AEGVAPTTRE WAGTPILLND RGDIDLYYTC VTPGATIAKV RGKIVTSDQS VSLEGFQQVT
SLFSADGTIY QTEEQNAFWN FRDPSPFIDR NDGKLYMLFE GNVAGPRGSH EITQAEMGNV
PPGYEDVGGA KYQAGCVGLA VAKDLSGSEW QILPPLITAV GVNDQTERPH FVFQDGKYYL
FTISHKYTFA DNLTGPDGVY GFVSDKLTGP YTPMNSSGLV LGNPSSQPFQ TYSHYVMPNG
LVTSFIDSVP WKGKDYRIGG TEAPTVKILL KGDRSFIVDS FDYGYIPAMK DITLK