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Entry: A0A2C9U3E5_MANES
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ID   A0A2C9U3E5_MANES        Unreviewed;      1019 AA.
AC   A0A2C9U3E5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Name=SPS4 {ECO:0000313|EMBL:QAY30717.1};
GN   ORFNames=MANES_18G109400 {ECO:0000313|EMBL:OAY23815.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY23815.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY23815.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY23815.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QAY30717.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Huang T., Luo X., Wei M., Shan Z.;
RT   "Cloning and Expression Analysis of Sucrose Phosphate Synthase Gene Family
RT   in Cassava(Manihot esculenta).";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; CM004404; OAY23815.1; -; Genomic_DNA.
DR   EMBL; MK181570; QAY30717.1; -; mRNA.
DR   AlphaFoldDB; A0A2C9U3E5; -.
DR   STRING; 3983.A0A2C9U3E5; -.
DR   EnsemblPlants; OAY23815; OAY23815; MANES_18G109400.
DR   Gramene; OAY23815; OAY23815; MANES_18G109400.
DR   OMA; YEAHVEY; -.
DR   OrthoDB; 1206157at2759; -.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000091857; Chromosome lg18.
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; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR   PANTHER; PTHR46039:SF1; SUCROSE-PHOSPHATE SYNTHASE 4; 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   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT   DOMAIN          251..396
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          471..644
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          783..953
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   REGION          117..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  115297 MW;  55474617045218C5 CRC64;
     MAGNDWINGY LEAILDVGSS LRKRNDGQLK ISKFEDSKQK EDKSFSPTKY FVEEVINSFD
     ESDLHRTWVK VIATRNTRER SNRLENMCWR IWHLARMKKK IEWDDAQRLA RRRLEREQGR
     NDAADDLSEL SEGEKEKGDT NLSEPVKNFS RINSDMQIWS DEEKPRRLYI VLISMHGLVR
     GENMELGRDS DTGGQVKYVV ELARALANTK GVYRVDLLTR QISSPEVDYS YGEPIEMLAC
     PPDGSGSCGA YIVRIPCGPR EKYIPKESLW PYIPEFVDGA LSHIVNMARA LGEQVNGGKP
     TWPYVIHGHY ADAGEVASHL SGALNVPMVL TGHSLGRNKF EQLLKQGRLS KEDINVTYKI
     MRRIEAEELG LDATEMVVTS TKQEIEEQWG LYDGFDIKLE RKLRVRRRRG VSCMGRHMPR
     MVVIPPGMDF SYVTTHDSLE GDLKSLIGPD RTQTKRNLPP IWSEVMRFFT NPHKPTILAL
     SRPDPKKNVT TLLKAFGECQ RLRELANLTL ILGNRDDIEE MSNSSSVVLT TVLKLIDKYD
     LYGQVAYPKH HKQSEVPDIY RLAAKTKGVF INPALVEPFG LTLIEAAAYG LPVVATKNGG
     PVDILKALNN GLLVDPHDQK AIADALLKLV ADKNLWTECR KNGLKNIHRF SWPEHCRNYL
     SHIEHCRNRH PTSRLEITPV PEEPMSDSLK DVEDLSLRFS IEGDPKLNGE LDATTRQKKL
     IEAITQAASF NGNTNVTYSP GRRQMLFVIA VDCYDCNGKS TETFQEIIKN VMKAAGSCLG
     LGRIGFVLST GSSLQETMEA LRYCPVNIED FDAIICNSGS EMYCPWRDMV ADLDYEAHVG
     YRWPGENVRS MAIRLAKVED GAEDDVLEYV QASGSRSYSY IIKPGAKTRK VDEIRQRLRM
     RGIRCSLVYT RAASRLNVIP LFASRKQALR YLSVRWGIDL SKIVVFVGEK GDTDYEELLA
     GLHKTLIMRG SVEYGSENLL CGQDGFKRED IIPQESPSLR FVEENYENLS TALETLGIK
//
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