SUS_THEVB
ID SUS_THEVB Reviewed; 808 AA.
AC Q8DK23;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sucrose synthase;
DE Short=SuSyTe;
DE EC=2.4.1.13 {ECO:0000269|PubMed:23196182};
GN Name=susA {ECO:0000303|PubMed:23196182}; OrderedLocusNames=tlr1047;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RA Torres L.L., Salerno G.L.;
RT "Expression, purification and characterization of a sucrose synthase gene
RT from Thermosynechococcus elongatus BP-1.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=23196182; DOI=10.1016/j.febslet.2012.11.011;
RA Figueroa C.M., Asencion Diez M.D., Kuhn M.L., McEwen S., Salerno G.L.,
RA Iglesias A.A., Ballicora M.A.;
RT "The unique nucleotide specificity of the sucrose synthase from
RT Thermosynechococcus elongatus.";
RL FEBS Lett. 587:165-169(2013).
CC -!- FUNCTION: Catalyzes the reversible conversion of sucrose and a
CC nucleotide disphosphate (NDP) into fructose and NDP-glucose; although
CC the reaction is freely reversible in vitro, the physiological reaction
CC seems to be sucrose cleavage. Unlike characterized plant enzymes
CC prefers ADP as a cosubstrate, whereas plants prefer UDP
CC (PubMed:23196182). Its preference for ADP over UDP suggests it may
CC directly link sucrose and glycogen metabolism (Probable).
CC {ECO:0000269|PubMed:23196182, ECO:0000305|PubMed:23196182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC Evidence={ECO:0000269|PubMed:23196182};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-alpha-D-glucose + D-fructose = ADP + H(+) + sucrose;
CC Xref=Rhea:RHEA:55080, ChEBI:CHEBI:15378, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216;
CC EC=2.4.1.13; Evidence={ECO:0000269|PubMed:23196182};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.033 mM for ADP-glucose for sucrose synthesis, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC KM=1.7 mM for UDP-glucose for sucrose synthesis, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Vmax=1.1 umol/min/mg enzyme for sucrose synthesis with ADP-glucose,
CC pH 7.0 {ECO:0000269|PubMed:23196182};
CC Vmax=2.9 umol/min/mg enzyme for sucrose synthesis with UDP-glucose,
CC pH 7.0 {ECO:0000269|PubMed:23196182};
CC Vmax=1.28 umol/min/mg enzyme for sucrose cleavage with ADP, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Vmax=3.8 umol/min/mg enzyme for sucrose cleavage with CDP, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Vmax=3.9 umol/min/mg enzyme for sucrose cleavage with GDP, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Vmax=1.41 umol/min/mg enzyme for sucrose cleavage with TDP, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Vmax=2.2 umol/min/mg enzyme for sucrose cleavage with UDP, pH 7.0
CC {ECO:0000269|PubMed:23196182};
CC Note=kcat/KM for sucrose synthesis is 70094 for ADP-gluce and 2673
CC for UDP-glucose.;
CC pH dependence:
CC Optimum pH is 7-9 for sucrose cleavage with ADP as substrate.
CC {ECO:0000269|PubMed:23196182};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius for sucrose degradation
CC with UDP and 70 degrees Celsius with ADP. The enzyme remains stable
CC for 10 minutes at 50 degrees Celsius, while addition of ADP, UDP or
CC sucrose enhances thermal stability by 5 degrees Celsius.
CC {ECO:0000269|PubMed:23196182};
CC -!- SUBUNIT: Probably a homotetramer (PubMed:23196182).
CC {ECO:0000305|PubMed:23196182}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; FJ457909; ACS32312.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC08600.1; -; Genomic_DNA.
DR RefSeq; NP_681838.1; NC_004113.1.
DR RefSeq; WP_011056890.1; NC_004113.1.
DR AlphaFoldDB; Q8DK23; -.
DR SMR; Q8DK23; -.
DR STRING; 197221.22294771; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; BAC08600; BAC08600; BAC08600.
DR KEGG; tel:tlr1047; -.
DR PATRIC; fig|197221.4.peg.1100; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; WISRFEI; -.
DR OrthoDB; 694191at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR000368; Sucrose_synth.
DR InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR PANTHER; PTHR45839; PTHR45839; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02470; sucr_synth; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..808
FT /note="Sucrose synthase"
FT /id="PRO_0000442259"
FT REGION 271..753
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P49040"
SQ SEQUENCE 808 AA; 93964 MW; F730297F8001316D CRC64;
MTCVLLKAVV ESDERADLRQ FSRILQLGEK RYLLRNDILD AFADYCRDQE RPVPPPSESR
LSKLVFYTQE IIVDNESLCW IVRPRIAQQE VCRLLVEDLT IVPMTIPELL DLRDRLVNHY
HPNEGDVFEI DVQPFYDYSP IIRDAKNIGK GVEFLNRYLS SKLFQDPRQW QQNLFNFLRI
HRYNGYQLLI NERIRSPQHL SEQVKQALVV LSDRPPTEAY SEFRFELQNL GFEPGWGNTV
ARVRDTLEIL DQLLDSPDHQ VLEAFVSRIP MLFRIALISP HGWFGQEGVL GRPDTGGQVV
YILDQVKSLE KQMREDLELA GLGVLEAQPK IIVLTRLIPN AEGTLCNQRL EKIYGTNDAW
ILRVPFREFN PKVTQNWISR FEIWPYLETF AIDAERELRA EFGHVPDLII GNYSDGNLVA
FLLARRLKVT QCNIAHALEK SKYLFSNLYW QDLEDKYHFS LQFTADLIAM NAANFIISST
YQEIVGTPDS IGQYESYQSF TMPDLYHVVN GIELFSPKFN VVPPGVNEQV YFPYYHYTER
LEGDRQRLEE LLFTLEDPQQ IYGYLEAPEK RPLFSMARLD RIKNLTGLAE AFGRSKALQE
RCNLILVAGK LRTADSSDRE EIAEIEKLYQ IIHQYNLHGK IRWLGIRLPK ADSGEIYRII
ADRQGIFVQP ALFEAFGLTI LEAMISGLPT FGTRFGGPLE IIQDGVNGFY INPTHLEEMA
ETIVRFLEAC DRDPQEWQRI SKAGIERVYS TYTWKIHCTR LLSLAKIYGF WNFSSQENRE
DMMRYMEALF HLLYKPRAQA LLAEHLQR
