ID V7CCI0_PHAVU Unreviewed; 1055 AA.
AC V7CCI0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=PHAVU_003G170100g {ECO:0000313|EMBL:ESW27058.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW27058.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002290; ESW27058.1; -; Genomic_DNA.
DR RefSeq; XP_007155064.1; XM_007155002.1.
DR AlphaFoldDB; V7CCI0; -.
DR STRING; 3885.V7CCI0; -.
DR EnsemblPlants; ESW27058; ESW27058; PHAVU_003G170100g.
DR GeneID; 18635174; -.
DR Gramene; ESW27058; ESW27058; PHAVU_003G170100g.
DR KEGG; pvu:PHAVU_003G170100g; -.
DR eggNOG; KOG0853; Eukaryota.
DR OMA; AWSKGIS; -.
DR OrthoDB; 1206157at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000000226; Chromosome 3.
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 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 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:UP000000226};
KW Transferase {ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 471..644
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 836..1001
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 93..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 117544 MW; 135C5746DF10D9B9 CRC64;
MAGNDWLNSY LEAILDVGPG LDDSKSSLLL RERGRFSPTR YFVEEVIGFD ETDLYRSWVR
ASSTRSPQER NTRLENMCWR IWNLARQKKQ LESETAQRLN KRRLERERGR REATADMSED
LSEGEKGDPV SDTSAHGDTY RARMPRISSA DAMESWANSQ KGKKLYIVLV SIHGLIRGEN
MELGRDSDTG GQVKYVVELA RALGSMPGVY RVDLLTRQVS APDVDWSYGE PTEMLTPRDS
DDFGDDMGES SGSYIVRIPF GPRDKYIPKE LLWPHIPEFV DGALNHIIQM SKSLGEQIGS
GHAIWPVAIH GHYADAGDSA ALLSGALNVP MLFTGHSLGR DKLEQLLKQG RLSRDEINAT
YKIMRRIEAE ELALDGSEIV ITSTRQEIEE QWRLYDGFDP VLERKIRARI RRNVSCYGRS
MPRMATIPPG MEFHHIVPQD GDIEGEPEGN LDHPAPQDPP IWSEIMRFFT NPRKPMILAL
ARPDPKKNIT TLVKAFGECR PLQELANLTL IMGNRDGIDE MSSTNASVLL SVLKLIDKYD
LYGQVAYPKH HKQSDVPDIY RLAAKTKGVF INPAFIEPFG LTLIEAAAHG LPTVATKNGG
PVDIVRVLDN GLLIDPHDEQ SIADALLKLV SNKQLWAKCR QNGLKNIHLF SWPEHCKTYL
SKIATCKPRH PQWQRIEDGG ESSESESPGD SLRDIQDLSL NMKFSLDGEK SGGSGNDNSL
DSDGNGADRK AKLENALLSW SKGISKDTRR GGATEKSDQN PNAGKFPPLR RRKHLFVIAV
DCDTTSGLLE TIKVIFESAG KDRAEGSIGF ILSTSLTISE IQSFLISGGL SPSDFDAYIC
NSGSDLYYPS LNPEDRPFVV DLYYHSHIEY RWGGEGLRKT LLRWADSITD KGGNNEQIVS
PAEQLSTDYC YAFKVRKPGM APPVKELRKL LRIQALRCHP IYCQNGTRLN VIPVLASRSQ
ALRYLYVRWG FELSKIVVFA GECGDTDYEG LLGGLHKSVI LKGVGSSAIS QLHNNRNYPL
SDVMPLDSPN IVEATEGSSG TDIQALIEKV GYLSG
//
