ID   SPSA2_CRAPL             Reviewed;        1081 AA.
AC   O04933;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Probable sucrose-phosphate synthase 2;
DE            EC=2.4.1.14;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase 2;
GN   Name=SPS2;
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; Y11795; CAA72491.1; -; mRNA.
DR   PIR; T09837; T09837.
DR   AlphaFoldDB; O04933; -.
DR   SMR; O04933; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; O04933; -.
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..1081
FT                   /note="Probable sucrose-phosphate synthase 2"
FT                   /id="PRO_0000204670"
FT   REGION          116..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  120934 MW;  DD142DC2F1A72900 CRC64;
     MAGNEWINGY LEAILDTGAS AIDENSGGGK TAAAQKGRHH DHHFNPTKYF VEEVVSGVDE
     SDLHRTWIKV VATRNTRERS SRLENMCWRI WHLTRKKKQL EWEDLQRLAA RKWEREQGRK
     DVTEDMSEDL SEGEKGDVMG ETPVALDSPR GNKKYHRNFS NLEVWSDSNK EKKLYIVLIS
     LHGLVRGENM ELGRDSDTGG QIKYVVEVAR ALAKMPGVYR VDLFTRQISS PEVDWSYAEP
     TEMLSSSSTT AGEAHEPEEE EEEEDLGEGS GAYIIRIPFG PRDKYLRKEL LWPHIQEFVD
     GALSHIVNMS KALGDQIGGG QPVWPYVIHG HYADAGDSAA LLSGALNVPM VLTGHSLGRN
     KLEQLLKQGR QTKEDINSMY RIMRRIEAEE LSLDAAELVI TSTKQEIEEQ WGLYDGFDVK
     LERVLRARAR RGVNCHGRFM PRMAVIPPGM DFSNVVVPED GSEGDGDLAT LTEATSPRSV
     PAIWADVMRF LTNPHKPMIL ALSRPDPKKN ITTLVKAFGE CRPLRELANL TLIMGNRDDI
     DEMSGGNASV LTTVLKLIDR YDLYGQVAFP KHHKQSDVPE IYRLASKTKG VFINPAFIEP
     FGLTLIEAAA HGLPMVATKN GGPVDIHRAL NNGLLVDPHD QDAIANALLK LVSEKNLWNE
     CRKNGLKNIH LFSWPEHCRT YLTRVAACRM RHPQWKTDTP LDETAIDDSL NDSLKDVLDM
     SLRLSVDGEK MSVNESSSVE LPGGEAAELP DQVRRVLNKI KRQDSGPAQR EAEGKAGDVP
     GKYPMLRRRR KLFVIALDCY DLKGNPDKKM ILSIQEIVRA VRLDPQMSRF SGFALSTAMP
     VAELADFLKA GDVKVNDFDA LICSSGSEVY YPGTYGEESG KLYLDPDYTS HIEYRWGGDG
     LKKTISKLMN TAEDGKSSVA SSPIELVAKS SNSHCLSYAI KDPSKAKKVD DMRQKLRMRG
     LRCHLMYCRN STSMQVVPLL ASRSQALRYL FVRWRLSVAN MYVILGETGD TDYEELISGT
     HKTLIMRGVV EKGSEELLRT AGSYLRDDVI PQDTPLIAYA DKGAKAEHIV ETFRQLSKAG
     M