SACB_ZYMMO
ID SACB_ZYMMO Reviewed; 423 AA.
AC P0DJA3; Q06487; Q5NQK6; Q60114; Q60116;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 42.
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=sacB; Synonyms=levU, sucE2; OrderedLocusNames=ZMO0374;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=7766026; DOI=10.1271/bbb.59.289;
RA Kyono K., Yanase H., Tonomura K., Kawasaki H., Sakai T.;
RT "Cloning and characterization of Zymomonas mobilis genes encoding
RT extracellular levansucrase and invertase.";
RL Biosci. Biotechnol. Biochem. 59:289-293(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RT "Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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 -!- PTM: Does not seem to be N-terminally processed.
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; D17524; BAA04475.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29870.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88998.1; -; Genomic_DNA.
DR PIR; JC2519; JC2519.
DR RefSeq; WP_011240294.1; NZ_CP035711.1.
DR AlphaFoldDB; P0DJA3; -.
DR SMR; P0DJA3; -.
DR STRING; 264203.ZMO0374; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR EnsemblBacteria; AAV88998; AAV88998; ZMO0374.
DR GeneID; 58026222; -.
DR KEGG; zmo:ZMO0374; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_031862_1_0_5; -.
DR OMA; DPWFFED; -.
DR OrthoDB; 1622507at2; -.
DR BRENDA; 2.4.1.10; 14380.
DR Proteomes; UP000001173; 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 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 Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW Secreted; Transferase.
FT CHAIN 1..423
FT /note="Levansucrase"
FT /id="PRO_0000057721"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 278
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 194
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT CONFLICT 39
FT /note="V -> I (in Ref. 1; BAA04475)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..203
FT /note="NPED -> TPKI (in Ref. 2; AAG29870)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="E -> Q (in Ref. 1; BAA04475)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="T -> A (in Ref. 1; BAA04475)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="C -> Y (in Ref. 1; BAA04475)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="I -> V (in Ref. 1; BAA04475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 46762 MW; 19A4691DA3EB9FE3 CRC64;
MLNKAGIAEP SLWTRADAMK VHTDDPTATM PTIDYDFPVM TDKYWVWDTW PLRDINGQVV
SFQGWSVIFA LVADRTKYGW HNRNDGARIG YFYSRGGSNW IFGGHLLKDG ANPRSWEWSG
CTIMAPGTAN SVEVFFTSVN DTPSESVPAQ CKGYIYADDK SVWFDGFDKV TDLFQADGLY
YADYAENNFW DFRDPHVFIN PEDGKTYALF EGNVAMERGT VAVGEEEIGP VPPKTETPDG
ARYCAAAIGI AQALNEARTE WKLLPPLVTA FGVNDQTERP HVVFQNGLTY LFTISHHSTY
ADGLSGPDGV YGFVSENGIF GPYEPLNGSG LVLGNPSSQP YQAYSHYVMT NGLVTSFIDT
IPSSDPNVYR YGGTLAPTIK LELVGHRSFV TEVKGYGYIP PQIEWLAEDE SSNSAAALSL
LNK