ID   SPSA1_CITUN             Reviewed;        1057 AA.
AC   O22060;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
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   Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=55188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Miyagawa-Wase; TISSUE=Juice tissue;
RX   PubMed=8842155; DOI=10.1007/bf02173781;
RA   Komatsu A., Takanokura Y., Omura M., Akihama T.;
RT   "Cloning and molecular analysis of cDNAs encoding three sucrose phosphate
RT   synthase isoforms from a citrus fruit (Citrus unshiu Marc.).";
RL   Mol. Gen. Genet. 252:346-351(1996).
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; AB005023; BAA23213.1; -; mRNA.
DR   PIR; S72648; S72648.
DR   AlphaFoldDB; O22060; -.
DR   SMR; O22060; -.
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   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR023214; HAD_sf.
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..1057
FT                   /note="Probable sucrose-phosphate synthase 1"
FT                   /id="PRO_0000204668"
FT   REGION          103..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1057 AA;  117900 MW;  447572147BDC16E9 CRC64;
     MAGNDWINSY LEAILDVGPG LDDAKSSLLL RERGRFSPTR YFVEEVITGF DETDLHRSWV
     KAQATRSPQE RNTRLENMCW RIWNLARQKK QLEGEAAQRM AKRRLERERG RREATADMSE
     DLSEGEKGDI VSDVSAHGDS TRSRLPRISS VDAMETWISQ QKGKKLYIVL ISIHGLIRGE
     NMELGRDSDT GGQVKYVVEL ARALGSMPGV YRVDLLTRQV SAPDVDWSYG EPTEMLTPRN
     SDDFMDDMGE SSGAYIIRIP FGPKDKYIAK ELLWPHIPEF VDGALNHIIR MSNVLGEQIG
     GGKPVWPVAI HGHYADAGDS AALLSGALNV PMLFTGHSLG RDKLEQLLKQ ARLSRDEINA
     TYKIMRRIEA EELSLDASEI VITSTRQEIE EQWRLYDGFD PVLERKLRAR IKRNVSCYGK
     FMPRMAIIPP GMEFHHIVPQ DGDMDGETEG NEDNPASPDP PIWSEIMRFF TNPRKPVILA
     LARPDPKKNI TTLVKAFGEC RPLRELANLT LIMGNRDGID EMSSTSASVL LSVLKLIDKY
     DLYGQVAYPK HHKQSDVPEI YRLAAKTKGV FINPAFIEPF GLTLIEAAAH GLPIVATKNG
     GPVDIHRVLD NGLLVDPHDQ QSIADALLKL VAGKQLWARC RQNGLKNIHL FSWPEHCKTY
     LSRIAGCKPR HPQWQRTDDG GETSESDSPG DSLRDIQDIS LNLKFSLDGE KSGASGNDDS
     LDSEGNVADR KSRLENAVLA WSKGVLKDTR KSGSTDKVDQ NTGAAKFPAL RRRKHIFVIS
     VDCDSTTGLL DATKKICEAV EKERTEGSIG FILSTSMTIS EIHSFLVSGH LSPSDFDAFI
     CNSGSDLYYS TLNSEDGPFV VDFYYHSHIE YRWGGEGLRK TLVRWASQVT DKKAESGEKV
     LTPAEQLSTN YCYAFSVQKP GMTPPVKELR KVLRIQALRC HVIYCQNGSR VNVIPVLASR
     SQALRYLYLR WGVELSKMVV FVGESGDTDY EGLLGGVHKT VILKGICSSS SNQIHANRSY
     PLSDVMPIDS PNIVQTPEDC TTSDIRSSLE QLGLLKV