ID   SPSA_BETVU              Reviewed;        1045 AA.
AC   P49031;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tap root;
RX   PubMed=7770061; DOI=10.1007/bf00293155;
RA   Hesse H., Sonnewald U., Willmitzer L.;
RT   "Cloning and expression analysis of sucrose-phosphate synthase from sugar
RT   beet (Beta vulgaris L.).";
RL   Mol. Gen. Genet. 247:515-520(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   -!- TISSUE SPECIFICITY: Predominantly active in tap root.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR   EMBL; X81975; CAA57500.1; -; mRNA.
DR   PIR; S55253; S55253.
DR   RefSeq; NP_001289997.1; NM_001303068.1.
DR   AlphaFoldDB; P49031; -.
DR   SMR; P49031; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; P49031; -.
DR   GeneID; 104901950; -.
DR   KEGG; bvg:104901950; -.
DR   UniPathway; UPA00371; UER00545.
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:0071836; P:nectar secretion; IEA:EnsemblPlants.
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; Transferase.
FT   CHAIN           1..1045
FT                   /note="Probable sucrose-phosphate synthase"
FT                   /id="PRO_0000204667"
FT   REGION          93..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1045 AA;  118181 MW;  8AEC555A5F805307 CRC64;
     MAGNDWINSY LEAILDVGPG LDDAKSSLLL RERGRFSPTR YFVEEVITGF DETDLHRSWV
     RAQATRSPQE RNTRLENMCW RIWNLARQKK QLENEEAQRK TKRRMELERG RREATADMSE
     DLSEGEKDIS AHGDSTRPRL PRINSLDAME TWISQQKEKK LYLVLISLHG LIRGENMELG
     RDSDTGGQVK YVVELARALG SMPGVYRVDL LTRQVSSPDV DWSYGEPTEM LNPRDSNGFD
     DDDDEMGESS GAYIVRIPFG PRDKYIAKEE LWPYIPEFVD GALNHIVQMS KVLGEQIGSG
     ETVWPVAIHG HYADAGDSAA LLSGGLNVPM LLTGHSLGRD KLEQLLKQGR MSKDDINNTY
     KIMRRIEAEE LSLDASEIVI TSTRQEIEEQ WHLYDGFDPV LERKLRARMK RGVSCYGRFM
     PRMVVIPPGM EFNHIVPHEG DMDGETEETE EHPTSPDPPI WAEIMRFFSK PRKPMILALA
     RPDPKKNITT LVKAFGECRP LRELANLTLI MGNRDGIDEM SSTSSSVLLS VLKLIDQYDL
     YGQVAYPKHH KQADVPEIYR LAAKTKGVFI NPAFIEPFGL TLIEAAAHGL PMVATKNGGP
     VDIQRVLDNG LLVDPHEQQS IATALLKLVA DKQLWTKCQQ NGLKNIHLYS WPEHSKTYLS
     RIASSRQRQP QWQRSSDEGL DNQEPESPSD SLRDIKDISL NLEVLVRPEK RVKTLKILGL
     MTKANSRMLL CSWSNGVHKM LRKARFSDKV DQASSKYPAF RRRKLIYVIA VDGDYEDGLF
     DIVRRIFDAA GKEKIEGSIG FILSTSYSMP EIQNYLLSKG FNLHDFDAYI CNSGSELYYS
     SLNSEESNII ADSDYHSHIE YRWGGEGLRR TLLRWAASIT EKNGENEEQV ITEDEEVSTG
     YCFAFKIKNQ NKVPPTKELR KSMRIQALRC HVIYCQNGSK MNVIPVLASR SQALRYLYVR
     WGVELSKMVV FVGECGDTDY EGLLGGVHKT VILKGVSNTA LRSLHANRSY PLSHVVSLDS
     PNIGEVSKGC SSSEIQSIVT KLSKA