ID   SUS1_SOLTU              Reviewed;         805 AA.
AC   P10691;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Sucrose synthase;
DE            EC=2.4.1.13;
DE   AltName: Full=SS16;
DE   AltName: Full=Sucrose-UDP glucosyltransferase;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sirtema;
RX   PubMed=2964386; DOI=10.1016/0378-1119(87)90212-5;
RA   Salanoubat M., Belliard G.;
RT   "Molecular cloning and sequencing of sucrose synthase cDNA from potato
RT   (Solanum tuberosum L.): preliminary characterization of sucrose synthase
RT   mRNA distribution.";
RL   Gene 60:47-56(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. FL1607; TISSUE=Leaf;
RX   PubMed=8589622; DOI=10.2307/3870128;
RA   Fu H., Park W.D.;
RT   "Sink- and vascular-associated sucrose synthase functions are encoded by
RT   different gene classes in potato.";
RL   Plant Cell 7:1369-1385(1995).
CC   -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC       fructose for various metabolic pathways.
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   -!- TISSUE SPECIFICITY: Expression is at least 10-fold higher in tubers
CC       compared to photosynthetically active tissues.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; M18745; AAA33841.1; -; mRNA.
DR   EMBL; U24087; AAA97571.1; -; Genomic_DNA.
DR   PIR; A29615; YUPOS.
DR   AlphaFoldDB; P10691; -.
DR   SMR; P10691; -.
DR   STRING; 4113.PGSC0003DMT400007505; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; P10691; -.
DR   ProMEX; P10691; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   BRENDA; 2.4.1.13; 5757.
DR   SABIO-RK; P10691; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P10691; baseline.
DR   GO; GO:0016157; F:sucrose synthase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..805
FT                   /note="Sucrose synthase"
FT                   /id="PRO_0000204661"
FT   REGION          275..752
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
FT   CONFLICT        221
FT                   /note="E -> D (in Ref. 2; AAA97571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        731..732
FT                   /note="KD -> RE (in Ref. 2; AAA97571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        741
FT                   /note="M -> T (in Ref. 2; AAA97571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="E -> Q (in Ref. 2; AAA97571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        759
FT                   /note="S -> R (in Ref. 2; AAA97571)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   805 AA;  92416 MW;  C453363A7CD32809 CRC64;
     MAERVLTRVH SLRERVDATL AAHRNEILLF LSRIESHGKG ILKPHELLAE FDAIRQDDKN
     KLNEHAFEEL LKSTQEAIVL PPWVALAIRL RPGVWEYIRV NVNALVVEEL SVPEYLQFKE
     ELVDGASNGN FVLELDFEPF TASFPKPTLT KSIGNGVEFL NRHLSAKMFH DKESMTPLLE
     FLRAHHYKGK TMMLNDRIQN SNTLQNVLRK AEEYLIMLPP ETPYFEFEHK FQEIGLEKGW
     GDTAERVLEM VCMLLDLLEA PDSCTLEKFL GRIPMVFNVV ILSPHGYFAQ ENVLGYPDTG
     GQVVYILDQV PALEREMLKR IKEQGLDIIP RILIVTRLLP DAVGTTCGQR IEKVYGAEHS
     HILRVPFRTE KGIVRKWISR FEVWPYMETF IEDVAKEISA ELQAKPDLII GNYSEGNLAA
     SLLAHKLGVT QCTIAHALEK TKYPDSDIYW KKFDEKYHFS SQFTADLIAM NHTDFIITST
     FQEIAGSKDT VGQYESHMAF TMPGLYRVVH GINVFDPKFN IVSPGADINL YFSYSETEKR
     LTAFHPEIDE LLYSDVENDE HLCVLKDRTK PILFTMARLD RVKNLTGLVE WYAKNPRLRG
     LVNLVVVGGD RRKESKDLEE QAEMKKMYEL IETHNLNGQF RWISSQMNRV RNGELYRYIA
     DTKGAFVQPA FYEAFGLTVV EAMTCGLPTF ATNHGGPAEI IVHGKSGFHI DPYHGEQAAD
     LLADFFEKCK KDPSHWETIS MGGLKRIEEK YTWQIYSESL LTLAAVYGFW KHVSKLDRLE
     IRRYLEMFYA LKYRKMAEAV PLAAE