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Protein

Sucrose-phosphate synthase 1

Gene

SPS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation. Required for nectar secretion.4 Publications

Catalytic activityi

UDP-glucose + D-fructose 6-phosphate = UDP + sucrose 6(F)-phosphate.

Enzyme regulationi

Activity is regulated by phosphorylation and moderated by concentration of metabolites and light.By similarity

Pathwayi: sucrose biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sucrose from D-fructose 6-phosphate and UDP-alpha-D-glucose.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable sucrose-phosphate synthase 3 (SPS3), Probable sucrose-phosphate synthase 4 (SPS4), Probable sucrose-phosphate synthase 2 (SPS2), Sucrose-phosphate synthase 1 (SPS1)
  2. Probable sucrose-phosphatase 3b (SPP3B), Probable sucrose-phosphatase 1 (SPP1), Probable sucrose-phosphatase 2 (SPP2), Probable sucrose-phosphatase 3a (SPP3A)
This subpathway is part of the pathway sucrose biosynthesis, which is itself part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sucrose from D-fructose 6-phosphate and UDP-alpha-D-glucose, the pathway sucrose biosynthesis and in Glycan biosynthesis.

GO - Molecular functioni

  • sucrose-phosphate synthase activity Source: TAIR
  • sucrose synthase activity Source: InterPro

GO - Biological processi

  • nectar secretion Source: UniProtKB
  • sucrose biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00371; UER00545.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrose-phosphate synthase 1 (EC:2.4.1.14)
Alternative name(s):
Sucrose-phosphate synthase 1F
Short name:
AtSPS1F
Sucrose-phosphate synthase 5.1
Short name:
AtSPS5.1
UDP-glucose-fructose-phosphate glucosyltransferase
Gene namesi
Name:SPS1
Synonyms:SPSA1
Ordered Locus Names:At5g20280
ORF Names:F5O24.170
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G20280.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Loss of nectar secretion accompanied by starch accumulation in nectaries.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10431043Sucrose-phosphate synthase 1PRO_0000413637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei155 – 1551PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ94BT0.
PRIDEiQ94BT0.

PTM databases

iPTMnetiQ94BT0.

Expressioni

Tissue specificityi

Expressed in seeds, stems, rosette leaves, flowers and siliques. Highly expressed in maturing nectaries.2 Publications

Inductioni

Circadian-regulated, with the highest expression at the end of the light period and the lowest at the end of the dark period (in 12 hours light/12 hours dark cycle). Induced by cold (at protein level).1 Publication

Gene expression databases

ExpressionAtlasiQ94BT0. baseline and differential.
GenevisibleiQ94BT0. AT.

Interactioni

Subunit structurei

Homodimer or homotetramer.By similarity

Protein-protein interaction databases

BioGridi17426. 6 interactions.
IntActiQ94BT0. 7 interactions.
STRINGi3702.AT5G20280.1.

Structurei

3D structure databases

ProteinModelPortaliQ94BT0.
SMRiQ94BT0. Positions 191-671.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000009685.
InParanoidiQ94BT0.
KOiK00696.
OMAiKTWVRTA.
PhylomeDBiQ94BT0.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR006380. SPP_N.
IPR000368. Sucrose_synth.
IPR012819. SucrsPsyn_pln.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF05116. S6PP. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02468. sucrsPsyn_pln. 1 hit.

Sequencei

Sequence statusi: Complete.

Q94BT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNDWVNSY LEAILDVGQG LDDARSSPSL LLRERGRFTP SRYFVEEVIT
60 70 80 90 100
GYDETDLHRS WVKAVATRSP QERNTRLENM CWRIWNLARQ KKQHEEKEAQ
110 120 130 140 150
RLAKRRLERE KGRREATADM SEEFSEGEKG DIISDISTHG ESTKPRLPRI
160 170 180 190 200
NSAESMELWA SQQKGNKLYL VLISLHGLIR GENMELGRDS DTGGQVKYVV
210 220 230 240 250
ELARALGSMP GVYRVDLLTR QVSSPDVDYS YGEPTEMLTP RDSEDFSDEM
260 270 280 290 300
GESSGAYIVR IPFGPKDKYI PKELLWPHIP EFVDGAMSHI MQMSNVLGEQ
310 320 330 340 350
VGVGKPIWPS AIHGHYADAG DATALLSGAL NVPMLLTGHS LGRDKLEQLL
360 370 380 390 400
RQGRLSKEEI NSTYKIMRRI EGEELSLDVS EMVITSTRQE IDEQWRLYDG
410 420 430 440 450
FDPILERKLR ARIKRNVSCY GRFMPRMVKI PPGMEFNHIV PHGGDMEDTD
460 470 480 490 500
GNEEHPTSPD PPIWAEIMRF FSNSRKPMIL ALARPDPKKN ITTLVKAFGE
510 520 530 540 550
CRPLRELANL ALIMGNRDGI DEMSSTSSSV LLSVLKLIDK YDLYGQVAYP
560 570 580 590 600
KHHKQSDVPD IYRLAAKSKG VFINPAIIEP FGLTLIEAAA HGLPMVATKN
610 620 630 640 650
GGPVDIHRVL DNGLLVDPHD QQSISEALLK LVADKHLWAK CRQNGLKNIH
660 670 680 690 700
QFSWPEHCKT YLSRITSFKP RHPQWQSDDG GDNSEPESPS DSLRDIQDIS
710 720 730 740 750
LNLKFSFDGS GNDNYMNQEG SSMDRKSKIE AAVQNWSKGK DSRKMGSLER
760 770 780 790 800
SEVNSGKFPA VRRRKFIVVI ALDFDGEEDT LEATKRILDA VEKERAEGSV
810 820 830 840 850
GFILSTSLTI SEVQSFLVSG GLNPNDFDAF ICNSGSDLHY TSLNNEDGPF
860 870 880 890 900
VVDFYYHSHI EYRWGGEGLR KTLIRWASSL NEKKADNDEQ IVTLAEHLST
910 920 930 940 950
DYCYTFTVKK PAAVPPVREL RKLLRIQALR CHVVYSQNGT RINVIPVLAS
960 970 980 990 1000
RIQALRYLFV RWGIDMAKMA VFVGESGDTD YEGLLGGLHK SVVLKGVSCS
1010 1020 1030 1040
ACLHANRSYP LTDVISFESN NVVHASPDSD VRDALKKLEL LKD
Length:1,043
Mass (Da):117,321
Last modified:December 1, 2001 - v1
Checksum:i7E24C7B6AA656FB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti874 – 8741I → V in BAF01930 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296825 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92824.1.
AY039911 mRNA. Translation: AAK64015.1.
AY079334 mRNA. Translation: AAL85065.1.
AK230113 mRNA. Translation: BAF01930.1.
RefSeqiNP_197528.1. NM_122035.2.
UniGeneiAt.22681.

Genome annotation databases

EnsemblPlantsiAT5G20280.1; AT5G20280.1; AT5G20280.
GeneIDi832150.
GrameneiAT5G20280.1; AT5G20280.1; AT5G20280.
KEGGiath:AT5G20280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296825 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92824.1.
AY039911 mRNA. Translation: AAK64015.1.
AY079334 mRNA. Translation: AAL85065.1.
AK230113 mRNA. Translation: BAF01930.1.
RefSeqiNP_197528.1. NM_122035.2.
UniGeneiAt.22681.

3D structure databases

ProteinModelPortaliQ94BT0.
SMRiQ94BT0. Positions 191-671.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17426. 6 interactions.
IntActiQ94BT0. 7 interactions.
STRINGi3702.AT5G20280.1.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

PTM databases

iPTMnetiQ94BT0.

Proteomic databases

PaxDbiQ94BT0.
PRIDEiQ94BT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G20280.1; AT5G20280.1; AT5G20280.
GeneIDi832150.
GrameneiAT5G20280.1; AT5G20280.1; AT5G20280.
KEGGiath:AT5G20280.

Organism-specific databases

TAIRiAT5G20280.

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000009685.
InParanoidiQ94BT0.
KOiK00696.
OMAiKTWVRTA.
PhylomeDBiQ94BT0.

Enzyme and pathway databases

UniPathwayiUPA00371; UER00545.

Miscellaneous databases

PROiQ94BT0.

Gene expression databases

ExpressionAtlasiQ94BT0. baseline and differential.
GenevisibleiQ94BT0. AT.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR006380. SPP_N.
IPR000368. Sucrose_synth.
IPR012819. SucrsPsyn_pln.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF05116. S6PP. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02468. sucrsPsyn_pln. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1043.
    Strain: cv. Columbia.
  5. "Decreased expression of two key enzymes in the sucrose biosynthesis pathway, cytosolic fructose-1,6-bisphosphatase and sucrose phosphate synthase, has remarkably different consequences for photosynthetic carbon metabolism in transgenic Arabidopsis thaliana."
    Strand A., Zrenner R., Trevanion S., Stitt M., Gustafsson P., Gardestroem P.
    Plant J. 23:759-770(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Phylogenetic and expression analysis of sucrose phosphate synthase isozymes in plants."
    Lutfiyya L.L., Xu N., D'Ordine R.L., Morrell J.A., Miller P.W., Duff S.M.
    J. Plant Physiol. 164:923-933(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  7. "Over-expression of an arabidopsis family A sucrose phosphate synthase (SPS) gene alters plant growth and fiber development."
    Park J.Y., Canam T., Kang K.Y., Ellis D.D., Mansfield S.D.
    Transgenic Res. 17:181-192(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-125 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Decrease in leaf sucrose synthesis leads to increased leaf starch turnover and decreased RuBP regeneration-limited photosynthesis but not Rubisco-limited photosynthesis in Arabidopsis null mutants of SPSA1."
    Sun J., Zhang J., Larue C.T., Huber S.C.
    Plant Cell Environ. 34:592-604(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  11. "Nectar secretion requires sucrose phosphate synthases and the sugar transporter SWEET9."
    Lin I.W., Sosso D., Chen L.-Q., Gase K., Kim S.-G., Kessler D., Klinkenberg P.M., Gorder M.K., Hou B.-H., Qu X.-Q., Carter C.J., Baldwin I.T., Frommer W.B.
    Nature 508:546-549(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSPSA1_ARATH
AccessioniPrimary (citable) accession number: Q94BT0
Secondary accession number(s): Q0WLS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: December 1, 2001
Last modified: April 13, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants silencing SPS1 show reduced shoot growth, leaf fresh weight and dry weight, and decreased leaf starch, leaf sugar levels and sucrose export rates (PubMed:10998187 and PubMed:21309792). Tobacco plants overexpressing Arabidopsis SPS1 show increased stem height and diameter, increased total dry weight and elevated concentrations of sink sucrose pools (PubMed:17415671).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.