SPSA1_ARATH
ID SPSA1_ARATH Reviewed; 1043 AA.
AC Q94BT0; Q0WLS7;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Sucrose-phosphate synthase 1;
DE EC=2.4.1.14;
DE AltName: Full=Sucrose-phosphate synthase 1F;
DE Short=AtSPS1F;
DE AltName: Full=Sucrose-phosphate synthase 5.1;
DE Short=AtSPS5.1;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS1; Synonyms=SPSA1; OrderedLocusNames=At5g20280; ORFNames=F5O24.170;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1043.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10998187; DOI=10.1046/j.1365-313x.2000.00847.x;
RA Strand A., Zrenner R., Trevanion S., Stitt M., Gustafsson P.,
RA Gardestroem P.;
RT "Decreased expression of two key enzymes in the sucrose biosynthesis
RT pathway, cytosolic fructose-1,6-bisphosphatase and sucrose phosphate
RT synthase, has remarkably different consequences for photosynthetic carbon
RT metabolism in transgenic Arabidopsis thaliana.";
RL Plant J. 23:759-770(2000).
RN [6]
RP GENE FAMILY.
RX PubMed=16876912; DOI=10.1016/j.jplph.2006.04.014;
RA Lutfiyya L.L., Xu N., D'Ordine R.L., Morrell J.A., Miller P.W., Duff S.M.;
RT "Phylogenetic and expression analysis of sucrose phosphate synthase
RT isozymes in plants.";
RL J. Plant Physiol. 164:923-933(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP FUNCTION.
RX PubMed=17415671; DOI=10.1007/s11248-007-9090-2;
RA Park J.Y., Canam T., Kang K.Y., Ellis D.D., Mansfield S.D.;
RT "Over-expression of an arabidopsis family A sucrose phosphate synthase
RT (SPS) gene alters plant growth and fiber development.";
RL Transgenic Res. 17:181-192(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-125 AND SER-152, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21309792; DOI=10.1111/j.1365-3040.2010.02265.x;
RA Sun J., Zhang J., Larue C.T., Huber S.C.;
RT "Decrease in leaf sucrose synthesis leads to increased leaf starch turnover
RT and decreased RuBP regeneration-limited photosynthesis but not Rubisco-
RT limited photosynthesis in Arabidopsis null mutants of SPSA1.";
RL Plant Cell Environ. 34:592-604(2011).
RN [12]
RP PHOSPHORYLATION AT SER-152.
RX PubMed=24924143; DOI=10.1021/pr5003164;
RA Wu X., Sklodowski K., Encke B., Schulze W.X.;
RT "A kinase-phosphatase signaling module with BSK8 and BSL2 involved in
RT regulation of sucrose-phosphate synthase.";
RL J. Proteome Res. 13:3397-3409(2014).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24670640; DOI=10.1038/nature13082;
RA Lin I.W., Sosso D., Chen L.-Q., Gase K., Kim S.-G., Kessler D.,
RA Klinkenberg P.M., Gorder M.K., Hou B.-H., Qu X.-Q., Carter C.J.,
RA Baldwin I.T., Frommer W.B.;
RT "Nectar secretion requires sucrose phosphate synthases and the sugar
RT transporter SWEET9.";
RL Nature 508:546-549(2014).
CC -!- FUNCTION: Plays a major 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 Required for nectar secretion. {ECO:0000269|PubMed:10998187,
CC ECO:0000269|PubMed:17415671, ECO:0000269|PubMed:21309792,
CC ECO:0000269|PubMed:24670640}.
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. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in seeds, stems, rosette leaves, flowers
CC and siliques. Highly expressed in maturing nectaries.
CC {ECO:0000269|PubMed:21309792, ECO:0000269|PubMed:24670640}.
CC -!- INDUCTION: Circadian-regulated, with the highest expression at the end
CC of the light period and the lowest at the end of the dark period (in 12
CC hours light/12 hours dark cycle). Induced by cold (at protein level).
CC {ECO:0000269|PubMed:21309792}.
CC -!- PTM: Phosphorylated at Ser-152 upon sucrose supply.
CC {ECO:0000269|PubMed:24924143}.
CC -!- DISRUPTION PHENOTYPE: Loss of nectar secretion accompanied by starch
CC accumulation in nectaries. {ECO:0000269|PubMed:24670640}.
CC -!- MISCELLANEOUS: Plants silencing SPS1 show reduced shoot growth, leaf
CC fresh weight and dry weight, and decreased leaf starch, leaf sugar
CC levels and sucrose export rates (PubMed:10998187 and PubMed:21309792).
CC Tobacco plants overexpressing Arabidopsis SPS1 show increased stem
CC height and diameter, increased total dry weight and elevated
CC concentrations of sink sucrose pools (PubMed:17415671).
CC {ECO:0000305|PubMed:17415671}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92824.1; -; Genomic_DNA.
DR EMBL; AY039911; AAK64015.1; -; mRNA.
DR EMBL; AY079334; AAL85065.1; -; mRNA.
DR EMBL; AK230113; BAF01930.1; -; mRNA.
DR RefSeq; NP_197528.1; NM_122035.3.
DR AlphaFoldDB; Q94BT0; -.
DR SMR; Q94BT0; -.
DR BioGRID; 17426; 8.
DR IntAct; Q94BT0; 8.
DR STRING; 3702.AT5G20280.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q94BT0; -.
DR PaxDb; Q94BT0; -.
DR PRIDE; Q94BT0; -.
DR ProteomicsDB; 228366; -.
DR EnsemblPlants; AT5G20280.1; AT5G20280.1; AT5G20280.
DR GeneID; 832150; -.
DR Gramene; AT5G20280.1; AT5G20280.1; AT5G20280.
DR KEGG; ath:AT5G20280; -.
DR Araport; AT5G20280; -.
DR TAIR; locus:2149179; AT5G20280.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR InParanoid; Q94BT0; -.
DR OMA; DYCYTFT; -.
DR OrthoDB; 101620at2759; -.
DR PhylomeDB; Q94BT0; -.
DR BRENDA; 2.4.1.14; 399.
DR UniPathway; UPA00371; UER00545.
DR PRO; PR:Q94BT0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BT0; baseline and differential.
DR Genevisible; Q94BT0; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0071836; P:nectar secretion; IMP:UniProtKB.
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 PANTHER; PTHR46039; PTHR46039; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1043
FT /note="Sucrose-phosphate synthase 1"
FT /id="PRO_0000413637"
FT REGION 95..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24924143,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 874
FT /note="I -> V (in Ref. 4; BAF01930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1043 AA; 117321 MW; 7E24C7B6AA656FB8 CRC64;
MAGNDWVNSY LEAILDVGQG LDDARSSPSL LLRERGRFTP SRYFVEEVIT GYDETDLHRS
WVKAVATRSP QERNTRLENM CWRIWNLARQ KKQHEEKEAQ RLAKRRLERE KGRREATADM
SEEFSEGEKG DIISDISTHG ESTKPRLPRI NSAESMELWA SQQKGNKLYL VLISLHGLIR
GENMELGRDS DTGGQVKYVV ELARALGSMP GVYRVDLLTR QVSSPDVDYS YGEPTEMLTP
RDSEDFSDEM GESSGAYIVR IPFGPKDKYI PKELLWPHIP EFVDGAMSHI MQMSNVLGEQ
VGVGKPIWPS AIHGHYADAG DATALLSGAL NVPMLLTGHS LGRDKLEQLL RQGRLSKEEI
NSTYKIMRRI EGEELSLDVS EMVITSTRQE IDEQWRLYDG FDPILERKLR ARIKRNVSCY
GRFMPRMVKI PPGMEFNHIV PHGGDMEDTD GNEEHPTSPD PPIWAEIMRF FSNSRKPMIL
ALARPDPKKN ITTLVKAFGE CRPLRELANL ALIMGNRDGI DEMSSTSSSV LLSVLKLIDK
YDLYGQVAYP KHHKQSDVPD IYRLAAKSKG VFINPAIIEP FGLTLIEAAA HGLPMVATKN
GGPVDIHRVL DNGLLVDPHD QQSISEALLK LVADKHLWAK CRQNGLKNIH QFSWPEHCKT
YLSRITSFKP RHPQWQSDDG GDNSEPESPS DSLRDIQDIS LNLKFSFDGS GNDNYMNQEG
SSMDRKSKIE AAVQNWSKGK DSRKMGSLER SEVNSGKFPA VRRRKFIVVI ALDFDGEEDT
LEATKRILDA VEKERAEGSV GFILSTSLTI SEVQSFLVSG GLNPNDFDAF ICNSGSDLHY
TSLNNEDGPF VVDFYYHSHI EYRWGGEGLR KTLIRWASSL NEKKADNDEQ IVTLAEHLST
DYCYTFTVKK PAAVPPVREL RKLLRIQALR CHVVYSQNGT RINVIPVLAS RIQALRYLFV
RWGIDMAKMA VFVGESGDTD YEGLLGGLHK SVVLKGVSCS ACLHANRSYP LTDVISFESN
NVVHASPDSD VRDALKKLEL LKD
