ID B9T123_RICCO Unreviewed; 998 AA.
AC B9T123;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
GN ORFNames=RCOM_0271410 {ECO:0000313|EMBL:EEF30424.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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 {ECO:0000256|RuleBase:RU368006}.
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 Evidence={ECO:0000256|ARBA:ARBA00001481,
CC ECO:0000256|RuleBase:RU368006};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005027, ECO:0000256|RuleBase:RU368006}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|ARBA:ARBA00011774,
CC ECO:0000256|RuleBase:RU368006}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00006530, ECO:0000256|RuleBase:RU368006}.
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DR EMBL; EQ974322; EEF30424.1; -; Genomic_DNA.
DR AlphaFoldDB; B9T123; -.
DR STRING; 3988.B9T123; -.
DR eggNOG; KOG0853; Eukaryota.
DR InParanoid; B9T123; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03800; GT4_sucrose_synthase; 1.
DR CDD; cd16419; HAD_SPS; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR NCBIfam; TIGR02468; sucrsPsyn_pln; 1.
DR PANTHER; PTHR46039:SF2; SUCROSE-PHOSPHATE SYNTHASE 1; 1.
DR PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368006};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 107..374
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 412..586
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 720..928
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 112011 MW; B6A43E9A05CE10ED CRC64;
MAGNDWINSY LEAILDVGPG LDDAKSSLLL RERGRFSPTR YFVEQVITGF DETDLHRSWA
RAQATRSPQE RNTRLENMCW RIWNLARQKK QVGFCYETYP DYDVRIQIVI FPILHGLIRG
ENMELGRDSD TGGQVKYVVE LARALGSMPG VYRVDLLTRQ VSSPDVDWSY GEPTEMLTLR
NLENFEDEMG ESSGAYIVRI PFGPRDKYVP KELLWPHIPE FVDGALNHII QMSKVLGEQI
GGGKPIWPVA IHGHYADAGD SAALLSGALN VPMLFTGHSL GRDKLEQLLK QGRLSRDEIN
LTYKIMRRIE AEEFSLDSSE IVITSTRQEI DEQWRLYDGF DPILERKLRA RIKRNVSCYG
RFMPRMAIIP PGMEFHHIVP QEGDMDGEIE GNEDHPTSPD PPIWTEIMRF FTNPRKPMIL
ALARPDPKKN ITTLVKAFGE CRPLRELANL TLVMGNRDGI DEMSSTNASV LLSVLKLIDK
YDLYGQVAYP KHHKQSDVPD IYRLAAKTKG VFINPAFIEP FGLTLIEAAA HGLPIVATKN
GGPVDIHRVL DNGLLVDPHD QQSIADALLK LVADKQLWEK CRQNGLKNIH LFSWPEHCKS
YLSRIASCKP RHPKWEKNND GGDTSDTDSP GDSLRDIHDL SLNLKFSLDG EKTGASGTDN
SLEYEGDGSD KKTKIENAVL AWSKGVSKNT QKMGSTEKGE HNNSSGKFPA LRRRKQIFVI
AVDFDNISVL LEATRKIFDA VERERTEGSI GFILSTSLTI SEIHSFLVSG GFSPSDFDAF
ICNSGSDLYY SNHNPEDGPF VVDFYYHSHI EYRWGGEGLR KTLVRWAASV NDKKSKNEEH
IVTAAEQLST NYCYAFKVQT PGLVPPVKEL RKLLRIQALR SHVIYCQNGT RINVIPVLAS
RSQALRYLYV RWGVELANMV IFVGECGDTD YEGLLGGIHK SIILKGVCCG ANNQLHANRN
YPLSDVIPSD NSNVVQTAEE CTCSDILGSL EQLGCLKG
//