ID Q9L466_LEUME Unreviewed; 1477 AA.
AC Q9L466;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=dextransucrase {ECO:0000256|ARBA:ARBA00012592};
DE EC=2.4.1.5 {ECO:0000256|ARBA:ARBA00012592};
DE AltName: Full=Dextransucrase {ECO:0000256|ARBA:ARBA00029911};
DE AltName: Full=Sucrose 6-glucosyltransferase {ECO:0000256|ARBA:ARBA00032238};
GN Name=dsrC {ECO:0000313|EMBL:CAB76565.1};
GN Synonyms=dsrb742 {ECO:0000313|EMBL:AAQ17210.1};
OS Leuconostoc mesenteroides.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1245 {ECO:0000313|EMBL:CAB76565.1};
RN [1] {ECO:0000313|EMBL:CAB76565.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL B-1355 {ECO:0000313|EMBL:CAB76565.1};
RA Arguello-Morales M.A., Remaud-Simeon M., Pizzut S., Sarcabal P.,
RA Willemot R.M., Monsan P.;
RT "Sequence analysis of the gene encoding alternansucrase, a sucrose
RT glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAQ17210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B-742CB {ECO:0000313|EMBL:AAQ17210.1};
RA Kim H., Kim D., Ryu H.-J., Robyt J.F.;
RT "Cloning and sequencing of the alpha 1-6 dextransucrase gene from
RT Leuconostoc mesenteroides B-742CB.";
RL J. Microbiol. Biotechnol. 10:559-563(2000).
RN [3] {ECO:0000313|EMBL:AAQ17210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B-742CB {ECO:0000313|EMBL:AAQ17210.1};
RA Kang H., Seo E., Ryu H.J., Robyt J.F., Kim D.;
RT "Directed evolution of a dextransucrase for increased constitutive activity
RT and the synthesis of a highly branched dextran.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAQ17210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B-742CB {ECO:0000313|EMBL:AAQ17210.1};
RX PubMed=16278932; DOI=10.1002/yea.1311;
RA Kang H.K., Kim S.H., Park J.Y., Jin X.J., Oh D.K., Kang S.S., Kim D.;
RT "Cloning and characterization of a dextranase gene from Lipomyces starkeyi
RT and its expression in Saccharomyces cerevisiae.";
RL Yeast 22:1239-1248(2005).
CC -!- FUNCTION: Production of extracellular glucans, that are thought to play
CC a key role in the development of the dental plaque because of their
CC ability to adhere to smooth surfaces and mediate the aggregation of
CC bacterial cells and food debris. {ECO:0000256|ARBA:ARBA00003243}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-
CC glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:18825, Rhea:RHEA-
CC COMP:11144, Rhea:RHEA-COMP:11145, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:18269, ChEBI:CHEBI:37721; EC=2.4.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 70 family.
CC {ECO:0000256|ARBA:ARBA00009247}.
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DR EMBL; AY280636; AAQ17210.1; -; Genomic_DNA.
DR EMBL; AJ250172; CAB76565.1; -; Genomic_DNA.
DR SMR; Q9L466; -.
DR CAZy; GH70; Glycoside Hydrolase Family 70.
DR BRENDA; 2.4.1.5; 839.
DR GO; GO:0047849; F:dextransucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046527; F:glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 5.
DR Gene3D; 2.30.30.420; glucansucrase; 1.
DR Gene3D; 3.20.20.470; Glucansucrase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR027636; Glucan-bd_rpt.
DR InterPro; IPR003318; Glyco_hydro70cat.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR04035; glucan_65_rpt; 5.
DR Pfam; PF01473; Choline_bind_1; 3.
DR Pfam; PF19127; Choline_bind_3; 5.
DR Pfam; PF02324; Glyco_hydro_70; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF69360; Cell wall binding repeat; 4.
DR PROSITE; PS51170; CW; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:CAB76565.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:CAB76565.1}.
FT DOMAIN 324..1117
FT /note="Glycoside hydrolase family 70 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02324"
FT REPEAT 1132..1152
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 164887 MW; E6F5710DEDFCB831 CRC64;
MLSMTATSQN VNADSTNTVT DKSVTVSNNS NTTNQHDTVV DKQTIPVKND QTTQQIAANA
TQAEKVKASD TTTDTQKQAE TANNTNKDSI DNLTKQLPAV TPTANQKTGY LEKDGKWYYV
TSDNTLAKGL TTVDNHKQYF DNNGVQAKGQ FVTDNSKTYY LDPNSGNAVT GIQQIGSQTL
AFNDNGEQVF ADFYTAPDGK TYYFDDKGQA TIGLKAINGH NYYFDSLGQL KKGFTGVIDG
QVRYFDQESG QEVSTTDSQI KEGLTSQTTD YTAHNAVHST DSADFDNFNG YLTASSWYRP
KDVLRNGQHW EATTANDFRP IVSVWWPSKQ TQVNYLNYMS QMGLIDNRQM FSLKDNQAML
NIACTTVQQA IETKIGVANS TAWLKTAIDD FIRTQPQWNM SSEDPKNDHL QNGALTFVNS
PLTPDTNSNF RLLNRTPTNQ TGVPKYTIDQ SKGGFELLLA NDVDNSNPVV QAEQLNWLHY
LMNFGSITAN DSAANFDGIR VDAVDNVDAD LLQIAADYFK AAYGVDKNDA TANQHLSILE
DWSHNDPEYV KDFGNNQLTM DDYMHTQLIW SLTKDMRMRG TMQRFMDYYL VNRNHDSTEN
TAIPNYSFVR AHDSEVQTVI AQIISELHPD VKNSLAPTAD QLAEAFKIYN NDEKQADKKY
TQYNMPSAYA MLLTNKDTVP RVYYGDLYTD DGQYMANKSP YFDAINGLLK SRIKYVAGGQ
SMAVDQNDIL TNVRYGKGAM SVTDSGNADT RTQGIGVIVS NKENLALKSG DTVTLHMGAA
HKNQAFRLLL GTTADNLSYY DNDNAPVKYT NDQGDLIFDN TEIYGVRNPQ VSGFLAVWVP
VGADSHQDAR TLSDDTAHHD GKTFHSNAAL DSQVIYEGFS NFQAFATNTE DYTNAVIAKN
GQLFKDWGIT SFQLAPQYRS STDTSFLDSI IQNGYAFTDR YDLGYGTPTK YGTVDQLRDA
IKALHANGIQ AIADWVPDQI YNLPGQELAT VTRTNSYGDK DTNSDIDQSL YVIQSRGGGK
YQAQYGGAFL SDIQKKYPAL FETKQISTGL PMDPSQKITE WSGKYFNGSN IQGKGAGYVL
KDSGTDQYYK VTSNNNNRDF LPKQLTDDLS ETGFVRDNIG MVYYTLSGYL ARNTFIQDDN
GNYYYFDSTG HLVTGFQNIN NHHYFFLPNG IELVQSFLQN ADGSTIYFDQ KGRQVFNQYI
TDQTGTAYYF QNDGTMVTSG FTEIDGHKQY FYKNGTQVKG QFVSDTDGHV FYLEAGNGNV
ATQRFAQNSQ GQWFYLGNDG IALTGLQTIN GVQNYFYADG HQSKGDFITI QNHVLYTNPL
TGAITTGMQQ IGDKIFVFDN TGNMLTNQYY QTLDGQWLHL STQGPADTGL VNINGNLKYF
QANGRQVKGQ FVTDPITNVS YYMNATDGSA VFNDYFTYQG QWYLTDSNYQ LVKGFKVVNN
KLQHFDEITG VQTKSAHIIV NNRTYIFDDQ GYFVSVA
//
