ID   SPSA1_CRAPL             Reviewed;        1054 AA.
AC   O04932;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Probable sucrose-phosphate synthase 1;
DE            EC=2.4.1.14;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase 1;
GN   Name=SPS1;
OS   Craterostigma plantagineum (Blue gem) (Torenia plantagineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Linderniaceae; Craterostigma.
OX   NCBI_TaxID=4153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9306694; DOI=10.1104/pp.115.1.113;
RA   Ingram J., Chandler J.W., Gallagher L., Salamini F., Bartels D.;
RT   "Analysis of cDNA clones encoding sucrose-phosphate synthase in relation to
RT   sugar interconversions associated with dehydration in the resurrection
RT   plant Craterostigma plantagineum Hochst.";
RL   Plant Physiol. 115:113-121(1997).
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; Y11821; CAA72506.1; -; mRNA.
DR   PIR; T09833; T09833.
DR   AlphaFoldDB; O04932; -.
DR   SMR; O04932; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
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: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..1054
FT                   /note="Probable sucrose-phosphate synthase 1"
FT                   /id="PRO_0000204669"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  119020 MW;  58558A387AE78BC4 CRC64;
     MAGNDWINSY LEAILDVGPG IDEAKGSLLL RERGRFSPTR YFVEEVVSGF DETDLHRSWI
     RAQATRSPQE RNTRLENMCW RIWNLARQKK QLENEEAQRM AKRRLERERG RREAVADMSE
     DLSEGEKGDI VVDHSHHGES NRGRLPRINS VDTMEAWMNQ QKGKKLYIVL ISLHGLIRGE
     NMELGRDSDT GGQVKYVVEL ARALGSMPGV YRVDLLTRQV SSPEVDWSYG EPTEMLPPRN
     SENMMDEMGE SSGSYIVRIP FGPKDKYVAK ELLWPHIPEF VDGALGHIIQ MSKVLGEQIG
     NGHPIWPAAI HGHYADAGDS AALLSGALNV PMLFTGHSLG RDKLEQLLRQ GRLSRDEINS
     TYKIMRRIEA EELSLDASEM VITSTRQEIE EQWRLYDGFD PILERKLRAR IKRNVSCYGR
     FMPRMMVIPP GMEFHHIVPH DGDLDAEPEF NEDSKSPDPH IWTEIMRFFS NPRKPMILAL
     ARPDPKKNLT TLVKAFGECK PLRELANLTL IMGNRDNIDE MSGTNASVLL SILKMIDKYD
     LYGLVAYPKH HKQSDVPDIY RLAAKTKGVF INPAFIEPFG LTLIEAAAHG LPIVATKNGG
     PVDIHRVLDN GILVDPHNQE SIADALLKLV AEKHLWAKCR ANGLKNIHLF SWPEHCKSYL
     SKLASCKPRQ PRWLRNEEDD DENSESDSPS DSLRDIQDIS LNLKFSFDGD KNESREKGGG
     SHPDDRASKI ENAVLEWSKG VAKGPQRSMS IEKGEHNSNA GKFPALRRRK IMFVIAVDCK
     PSAGLSESVR KVFAAVENER AEGSVGFILA TSFNISEIRH FLVSEKLNPT DFDAFICNSG
     GDLYYSSHHS EDNPFVVDLY YHSQIEYRWG GEGLRKTLVR WAASITDKKG EKEEHVIIED
     EETSADYCYS FKVQKPNVVP PVKEARKVMR IQALRCHVVY CQNGNKINVI PVLASRAQAL
     RYLYLRWGME LSKTVVVVGE SGDTDYEEML GGVHKTVVLS GVCTTATNLL HANRSYPLAD
     VVCFDDLNIF KTHNEECSST DLRALLEEHG AFKA