ID F6H3I4_VITVI Unreviewed; 1058 AA.
AC F6H3I4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
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 OrderedLocusNames=VIT_04s0008g05730 {ECO:0000313|EMBL:CCB46819.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB46819.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595231; CCB46819.1; -; Genomic_DNA.
DR RefSeq; XP_002282808.1; XM_002282772.3.
DR AlphaFoldDB; F6H3I4; -.
DR STRING; 29760.F6H3I4; -.
DR PaxDb; 29760-VIT_04s0008g05730-t01; -.
DR EnsemblPlants; Vitvi04g00508_t001; Vitvi04g00508_P001; Vitvi04g00508.
DR GeneID; 100244135; -.
DR Gramene; Vitvi04g00508_t001; Vitvi04g00508_P001; Vitvi04g00508.
DR KEGG; vvi:100244135; -.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR InParanoid; F6H3I4; -.
DR OrthoDB; 1206157at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000009183; Chromosome 4.
DR ExpressionAtlas; F6H3I4; baseline.
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:SF7; SUCROSE-PHOSPHATE SYNTHASE 2-RELATED; 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:UP000009183};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 167..433
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 472..645
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 799..991
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 100..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 117902 MW; 6F3DEBF5F53671C7 CRC64;
MAGNDWLNSY LEAIIDAGPN LGDAKSSLLL RERGHFSPTR YFVEEVITGF DETDLHRSWA
RASATRSPQE RNTRLENMCW RIWNLARKKK QLEGEEAQRV AKRHIDHERG RREATADMSE
DLSEGEKGDT VSDLPAQADN FKGQMRRINS IDVMENWASQ HKEKKLYIVL ISLHGLIRGE
NMELGRDSDT GGQVKYVVEL ARALGTMPGV YRVDLLTRQV SAPDVDWSYG EPAEMLHPVN
SENPVQEIGE SSGAYIIRIP FGPKDKYISK ELLWPHIPEF VDGALVHIIQ MSKVLGEQIG
NGQPVWPIAI HGHYADAGDS AALLSGAINV PMLFTGHSLG RDKLEQLLKQ GRQSNEEINA
TYKITRRIEA EELTLDASEV VITSTRQEIE QQWSLYNGFD PVIERKLRAR IRRNVSCLGR
FMPRMVIIPP GMEFHHIIPQ DGDMDGEIEG SGADPSSPDP PIWAEIMRFF TNPRKPMILA
LARADPKKNI TTLVKAFGEC RSLRELANLT LIMGNRDDID EMSSTNASVL ISILKLIDKY
DMYGQVAYPK HHKQSEVPEI YHLAAKTKGV FINPAFIEPF GLTLIEAAAH GLPIVATKNG
GPVDIHRVLD NGLLVDPHDQ QSVANALLKL VADKHLWGRC RQNGLKNIHL FSWPEHCKTY
LARIACCKQR HPEWQKPDDG FESSGSDSPG GSLRDIQDIS LNLKLSVGDE KNEVSRTLDN
YLDSEENAVD GKSKLENAVS SWSKGVSVGT QKDGSIYKSE HHIGSSKSPA LRKRKYIFVI
AVDGDGTTDF LESIKMVVET VRKDKYAGSV GFILSTSLAI SEMHSLLVSG GLSHSDFDAF
ICNSGTELYY PSSTSEDGTP GLPFLLDSDY HSHIEYRWGG EDLRKTLLRW AASTTDEKGE
GPIVSEDKSG STTHCYVFKV EKPELIPSIK ELRKSMRIQA LRCHVIYCQN GNKLNIIPVL
ASRSQALRYL HVRWGIDLSH VVVFVGEHGD TDYEGLLGGL HKTVILKGVG CSVGKHHAHR
YYPLEDVVPF DSPNITQTEG CNSNSIRASL GKLGVLKV
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