SPSA_MAIZE
ID SPSA_MAIZE Reviewed; 1068 AA.
AC P31927;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Sucrose-phosphate synthase {ECO:0000303|PubMed:1840396};
DE EC=2.4.1.14 {ECO:0000269|PubMed:1840396};
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase {ECO:0000303|PubMed:1840396};
GN Name=SPS {ECO:0000303|PubMed:1840396};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-74; 206-212; 471-481 AND
RP 872-892, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Pioneer 3184; TISSUE=Leaf;
RX PubMed=1840396; DOI=10.2307/3869300;
RA Worrell A.C., Bruneau J.-M., Summerfelt K., Boersig M., Voelker T.A.;
RT "Expression of a maize sucrose phosphate synthase in tomato alters leaf
RT carbohydrate partitioning.";
RL Plant Cell 3:1121-1130(1991).
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 (PubMed:1840396). Involved in the
CC regulation of carbon partitioning in the leaves of plants
CC (PubMed:1840396). May regulate the synthesis of sucrose and therefore
CC play a major role as a limiting factor in the export of
CC photoassimilates out of the leaf (PubMed:1840396). Plays a role for
CC sucrose availability that is essential for plant growth and fiber
CC elongation (PubMed:1840396). {ECO:0000269|PubMed:1840396}.
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:0000269|PubMed:1840396};
CC -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC moderated by concentration of metabolites and light.
CC {ECO:0000250|UniProtKB:P31928}.
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000269|PubMed:1840396}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:1840396}.
CC -!- DEVELOPMENTAL STAGE: Germinating seeds or mature leaves.
CC {ECO:0000269|PubMed:1840396}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; M97550; AAA33513.1; -; mRNA.
DR PIR; JQ1329; JQ1329.
DR RefSeq; NP_001105694.1; NM_001112224.1.
DR AlphaFoldDB; P31927; -.
DR SMR; P31927; -.
DR STRING; 4577.GRMZM5G875238_P01; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; P31927; -.
DR PRIDE; P31927; -.
DR EnsemblPlants; Zm00001eb364620_T001; Zm00001eb364620_P001; Zm00001eb364620.
DR GeneID; 542711; -.
DR Gramene; Zm00001eb364620_T001; Zm00001eb364620_P001; Zm00001eb364620.
DR KEGG; zma:542711; -.
DR MaizeGDB; 25294; -.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR OMA; VMNTTMD; -.
DR OrthoDB; 101620at2759; -.
DR BRENDA; 2.4.1.14; 6752.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; P31927; baseline and differential.
DR Genevisible; P31927; ZM.
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 Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..1068
FT /note="Sucrose-phosphate synthase"
FT /id="PRO_0000204671"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 118575 MW; 074679B5E9A1D282 CRC64;
MAGNEWINGY LEAILDSHTS SRGAGGGGGG GDPRSPTKAA SPRGAHMNFN PSHYFVEEVV
KGVDESDLHR TWIKVVATRN ARERSTRLEN MCWRIWHLAR KKKQLELEGI QRISARRKEQ
EQVRREATED LAEDLSEGEK GDTIGELAPV ETTKKKFQRN FSDLTVWSDD NKEKKLYIVL
ISVHGLVRGE NMELGRDSDT GGQVKYVVEL ARAMSMMPGV YRVDLFTRQV SSPDVDWSYG
EPTEMLCAGS NDGEGMGESG GAYIVRIPCG PRDKYLKKEA LWPYLQEFVD GALAHILNMS
KALGEQVGNG RPVLPYVIHG HYADAGDVAA LLSGALNVPM VLTGHSLGRN KLEQLLKQGR
MSKEEIDSTY KIMRRIEGEE LALDASELVI TSTRQEIDEQ WGLYDGFDVK LEKVLRARAR
RGVSCHGRYM PRMVVIPPGM DFSNVVVHED IDGDGDVKDD IVGLEGASPK SMPPIWAEVM
RFLTNPHKPM ILALSRPDPK KNITTLVKAF GECRPLRELA NLTLIMGNRD DIDDMSAGNA
SVLTTVLKLI DKYDLYGSVA FPKHHNQADV PEIYRLAAKM KGVFINPALV EPFGLTLIEA
AAHGLPIVAT KNGGPVDITN ALNNGLLVDP HDQNAIADAL LKLVADKNLW QECRRNGLRN
IHLYSWPEHC RTYLTRVAGC RLRNPRWLKD TPADAGADEE EFLEDSMDAQ DLSLRLSIDG
EKSSLNTNDP LWFDPQDQVQ KIMNNIKQSS ALPPSMSSVA AEGTGSTMNK YPLLRRRRRL
FVIAVDCYQD DGRASKKMLQ VIQEVFRAVR SDSQMFKISG FTLSTAMPLS ETLQLLQLGK
IPATDFDALI CGSGSEVYYP GTANCMDAEG KLRPDQDYLM HISHRWSHDG ARQTIAKLMG
AQDGSGDAVE QDVASSNAHC VAFLIKDPQK VKTVDEMRER LRMRGLRCHI MYCRNSTRLQ
VVPLLASRSQ ALRYLSVRWG VSVGNMYLIT GEHGDTDLEE MLSGLHKTVI VRGVTEKGSE
ALVRSPGSYK RDDVVPSETP LAAYTTGELK ADEIMRALKQ VSKTSSGM
