ID A0A3L6RJL5_PANMI Unreviewed; 1083 AA.
AC A0A3L6RJL5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=C2845_PM13G17330 {ECO:0000313|EMBL:RLN04709.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN04709.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN04709.1}.
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DR EMBL; PQIB02000008; RLN04709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6RJL5; -.
DR STRING; 4540.A0A3L6RJL5; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000275267; Chromosome 13.
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; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001296; Glyco_trans_1.
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; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR PANTHER; PTHR46039:SF5; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368006};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 188..452
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 494..666
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 811..1028
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 21..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..157
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1083 AA; 119397 MW; 05CFD0FB0A6B6BE8 CRC64;
MAGNEWINGY LEAILDSRTA PGGGGGGGGG GGGGGGGDPK SPVTGASPPA AASPRGPHMN
FNPTHYFVEE VVKGVDESDL HRTWIKVVAT RNARERSTRL ENMCWRIWHL ARKKKQLELE
GLQRMSAKRK EQEQVRREAT EDLAEDLSEA ADTLSELVPV ETAKKKFQRN FSDLTVWSDD
NKEKKLYIVL ISVHGLVRGE NMELGRDSDT GGQVKYVVEL ARALSMMPGV YRVDLFTRQV
SSPDVDWSYG EPTEMLTTGS IDGEGMGESG GAYIVRIPCG PRDKYLKKEA LWPYLQEFVD
GALGHILNMS KALGEQVGNG RPVLPYVIHG HYADAGDVAA LLSGALNVPM VLTGHSLGRN
KLEQLLKQGR MSKEDIDSTY KIMRRIEGEE LALDASELVI TSTRQEIDEQ WGLYDGFDVK
LEKVLRARTR RGVSCHGRFM PRMVVIPPGM DFSNVIPEDI DGDGDSKDDI ISLEGASPKS
MPPIWAEVMR FLTNPHKPMI LALSRPDPKK NITTLVKAFG ECRPLRELAN LTLIMGNRDD
IDEMSAGNAS VLTTVLKLID KYDLYGSVAF PKHHNQADVP EIYRLAAKMK GVFINPALVE
PFGLTLIEAA AHGLPIVATK NGGPVDITTA LNNGLLVDPH DQNAIADALL KLVADKNLWQ
ECRRNGLRNI HLYSWPEHCR TYLTRIAGCR LRNPRWLKDT PADAGADEEE LLEDSMDAQD
LSLRLSIDGE KNSLCINEPP SSDPQDQVQK IMNKIKQSSA LPPSMSSVSD GGKNAAEATG
SVVNKYPLLR RRRRLFVIAV DCYQDDGRAS KKMLQVIQEV LRAVRSDSQL SKISGFALST
AMPLSETLQL LQLGKIQATD FDALICGSGS EVYYPGTSHC IDAEGKLRPD QDYLLHISHR
WSQDGARQTI AKLMVAQDGS GDVVKQDVAS SNAHCVSFLI KDTKKVKTID EMRERLRMRG
LRCHIMYCRN STRLQVVPLL ASRSQALRYL FVRWGLAVGN MYLITGEHGD TDLEEMLSGL
HKTVVLRGVT EKGSEALLRS SGSYHRTDVV PTESPLVSYT AGDLKADEIM RALKQVSKTS
SGI
//
