ID   SPSA_SOLTU              Reviewed;        1053 AA.
AC   Q43845;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Probable sucrose-phosphate synthase;
DE            EC=2.4.1.14;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN   Name=SPS;
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. Desiree; TISSUE=Leaf;
RX   PubMed=7894514; DOI=10.1046/j.1365-313x.1995.07010097.x;
RA   Zrenner R., Salanoubat M., Willmitzer L., Sonnewald U.;
RT   "Evidence of the crucial role of sucrose synthase for sink strength using
RT   transgenic potato plants (Solanum tuberosum L.).";
RL   Plant J. 7:97-107(1995).
CC   -!- FUNCTION: Plays a role in photosynthetic sucrose synthesis by
CC       catalyzing the rate-limiting step of sucrose biosynthesis from UDP-
CC       glucose and fructose- 6-phosphate. Involved in the regulation of carbon
CC       partitioning in the leaves of plants. May regulate the synthesis of
CC       sucrose and therefore play a major role as a limiting factor in the
CC       export of photoassimilates out of the leaf. Plays a role for sucrose
CC       availability that is essential for plant growth and fiber elongation
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) +
CC         sucrose 6(F)-phosphate + UDP; Xref=Rhea:RHEA:22172,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.14;
CC   -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC       moderated by concentration of metabolites and light. {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC       fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR   EMBL; X73477; CAA51872.1; -; mRNA.
DR   PIR; S34172; S34172.
DR   AlphaFoldDB; Q43845; -.
DR   SMR; Q43845; -.
DR   STRING; 4113.PGSC0003DMT400071807; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   eggNOG; KOG0853; Eukaryota.
DR   InParanoid; Q43845; -.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43845; baseline.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR   GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16419; HAD_SPS; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR006380; SPP_N.
DR   InterPro; IPR044161; SPS.
DR   InterPro; IPR035659; SPS_C.
DR   InterPro; IPR012819; SPS_pln.
DR   InterPro; IPR000368; Sucrose_synth.
DR   PANTHER; PTHR46039; PTHR46039; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1053
FT                   /note="Probable sucrose-phosphate synthase"
FT                   /id="PRO_0000204673"
FT   REGION          103..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  118292 MW;  D6C933798567B20A CRC64;
     MAGNDWINSY LEAILDVGPG LDDKKSSLLL RERGRFSPTR YFVEEVITGF DETDLHRSWI
     RAQATRSPQR RNTRLENMCW RIWNLARQKK QLEGEQAQWM AKRRQERERG RREAVADMSE
     DLSEGEKGDI VADMSSHGES TRGRLPRISS VETMEAWVSQ QRGKKLYIVL ISLHGLIRGE
     NMELGRDSDT GGQVKYVVEL ARALGSMPGV YRVDLLTRQV SSPEVDWSYG EPTELAPIST
     DGLMTEMGES SGAYIIRIPF GPREKYIPKE QLWPYIPEFV DGALNHIIQM SKVLGEQIGS
     GYPVWPVAIH GHYADAGDSA ALLSGALNVP MLFTGHSLGR DKLEQLLAQG RKSKDEINST
     YKIMRRIEAE ELTLDASEIV ITSTRQEIDE QWRLYDGFDP ILERKLRARI KRNVSCYGRF
     MPRMAVIPPG MEFHHIVPHE GDMDGETEGS EDGKTPDPPI WAEIMRFFSN PRKPMILALA
     RPDPKKNLTT LVKAFGECRP LRDLANLTLI MGNRDNIDEM SSTNSALLLS ILKMIDKYDL
     YGQVAYPKHH KQSDVPDIYR LAAKTKGVFI NPAFIEPFGL TLIEAAAYGL PMVATKNGGP
     VDIHRVLDNG LLVDPHDQQA IADALLKLVA DKQLWAKCRA NGLKNIHLFS WPEHCKTYLS
     RIASCKPRQP RWLRSIDDDD ENSETDSPSD SLRDIHDISL NLRFSLDGEK NDNKENADNT
     LDPEVRRSKL ENAVLSLSKG ALKSTSKSWS SDKADQNPGA GKFPAIRRRR HIFVIAVDCD
     ASSGLSGSVK KIFEAVEKER AEGSIGFILA TSFNISEVQS FLLSEGMNPT DFDAYICNSG
     GDLYYSSFHS EQNPFVVDLY YHSHIEYRWG GEGLRKTLVR WAASIIDKNG ENGDHIVVED
     EDNSADYCYT FKVCKPGTVP PSKELRKVMR IQALRCHAVY CQNGSRINVI PVLASRSQAL
     RYLYLRWGMD LSKLVVFVGE SGDTDYEGLI GGLRKAVIMK GLCTNASSLI HGNRNYPLSD
     VLPFDSPNVI QADEECSSTE IRCLLEKLAV LKG