SPSA_SPIOL
ID SPSA_SPIOL Reviewed; 1056 AA.
AC P31928;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Sucrose-phosphate synthase;
DE EC=2.4.1.14;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8108511; DOI=10.1104/pp.102.2.529;
RA Salvucci M.E., Klein R.R.;
RT "Identification of the uridine-binding domain of sucrose-phosphate
RT synthase. Expression of a region of the protein that photoaffinity labels
RT with 5-azidouridine diphosphate-glucose.";
RL Plant Physiol. 102:529-536(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7763376; DOI=10.1007/bf00195074;
RA Sonnewald U., Quick W.P., Macrae E., Krause K.P., Stitt M.;
RT "Purification, cloning and expression of spinach leaf sucrose-phosphate
RT synthase in Escherichia coli.";
RL Planta 189:174-181(1993).
RN [3]
RP PROTEIN SEQUENCE OF 156-170, AND PHOSPHORYLATION AT SER-158.
RX PubMed=8274010; DOI=10.1006/abbi.1993.1586;
RA McMichael R.W. Jr., Klein R.R., Salvucci M.E., Huber S.C.;
RT "Identification of the major regulatory phosphorylation site in sucrose-
RT phosphate synthase.";
RL Arch. Biochem. Biophys. 307:248-252(1993).
RN [4]
RP FUNCTION, AND PHOSPHORYLATION AT SER-158 AND SER-424.
RX PubMed=9232876; DOI=10.1104/pp.114.3.947;
RA Toroser D., Huber S.C.;
RT "Protein phosphorylation as a mechanism for osmotic-stress activation of
RT sucrose-phosphate synthase in spinach leaves.";
RL Plant Physiol. 114:947-955(1997).
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:0000269|PubMed:9232876}.
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 -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC moderated by concentration of metabolites and light.
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-158 and Ser-424.
CC {ECO:0000269|PubMed:8274010, ECO:0000269|PubMed:9232876}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; L04803; AAA20092.1; -; mRNA.
DR EMBL; S54379; AAC60545.2; -; mRNA.
DR PIR; JQ2277; JQ2277.
DR AlphaFoldDB; P31928; -.
DR SMR; P31928; -.
DR IntAct; P31928; 1.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; P31928; -.
DR PRIDE; P31928; -.
DR OrthoDB; 101620at2759; -.
DR BioCyc; MetaCyc:MON-1742; -.
DR BRENDA; 2.4.1.14; 5812.
DR UniPathway; UPA00371; UER00545.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16419; HAD_SPS; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR006380; SPP_N.
DR InterPro; IPR044161; SPS.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR PANTHER; PTHR46039; PTHR46039; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosyltransferase; Phosphoprotein;
KW Transferase.
FT CHAIN 1..1056
FT /note="Sucrose-phosphate synthase"
FT /id="PRO_0000204674"
FT REGION 112..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8274010,
FT ECO:0000269|PubMed:9232876"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9232876"
FT CONFLICT 17
FT /note="V -> I (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..75
FT /note="RAASTRS -> ALHQLAG (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="A -> R (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
FT CONFLICT 643..644
FT /note="HL -> QV (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="R -> W (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038..1039
FT /note="DD -> EH (in Ref. 2; AAC60545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1056 AA; 117716 MW; 7443A1FD3F1AB336 CRC64;
MAGNDWINSY LEAILDVGGQ GIDASTGKTS TAPPSLLLRE RGHFSPSRYF VEEVISGFDE
TDLHRSWVRA ASTRSPQERN TRLENLCWRI WNLARKKKQI EGEEAQRLAK RHVERERGRR
EATADMSEDL SEGERGDTVA DMLFASESTK GRMRRISSVE MMDNWANTFK EKKLYVVLIS
LHGLIRGENM ELGRDSDTGG QVKYVVELAR ALGSMPGVYR VDLLTRQVSA PGVDWSYGEP
TEMLSSRNSE NSTEQLGESS GAYIIRIPFG PKDKYVAKEL LWPYIPEFVD GALSHIKQMS
KVLGEQIGGG LPVWPASVHG HYADAGDSAA LLSGALNVPM VFTGHSLGRD KLDQLLKQGR
LSREEVDATY KIMRRIEAEE LCLDASEIVI TSTRQEIEEQ WQLYHGFDLV LERKLRARMR
RGVSCHGRFM PRMAKIPPGM EFNHIAPEDA DMDTDIDGHK ESNANPDPVI WSEIMRFFSN
GRKPMILALA RPDPKKNLTT LVKAFGECRP LRELANLTLI IGNRDDIDEM STTSSSVLIS
ILKLIDKYDL YGQVAYPKHH KQSDVPDIYR LAAKTKGVFI NPAFIEPFGL TLIEAAAYGL
PIVATKNGGP VDIIGVLDNG LLIDPHDQKS IADALLKLVA DKHLWTKCRQ NGLKNIHLFS
WPEHCKNYLS RIASCKPRQP NWQRIDEGSE NSDTDSAGDS LRDIQDISLN LKLSLDAERT
EGGNSFDDSL DSEEANAKRK IENAVAKLSK SMDKAQVDVG NLKFPAIRRR KCIFVIALDC
DVTSDLLQVI KTVISIVGEQ RPTGSIGFIL STSMTLSEVD SLLDSGGLRP ADFDAFICNS
GSELYYPSTD YSESPFVLDQ DYYSHIDYRW GGEGLWKTLV KWAASVNEKK GENAPNIVIA
DETSSTTHCY AFKVNDFTLA PPAKELRKMM RIQALRCHAI YCQNGTRLNV IPVLASRSQA
LRYLFMRWGV ELSNFVVFVG ESGDTDYEGL LGGVHKTVIL KGIGSNTSNF HATRAYPMEH
VMPVDSPNMF QTGGCNIDDI SDALSKIGCL KAQKSL
