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Protein

Probable sucrose-phosphate synthase 2

Gene

SPS2

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

Functioni

Plays a 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.2 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

GO - Biological processi

  • nectar secretion Source: UniProtKB
  • pollen wall assembly 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:
Probable sucrose-phosphate synthase 2 (EC:2.4.1.14)
Alternative name(s):
Protein KAONASHI 2
Sucrose-phosphate synthase 2F
Short name:
AtSPS2F
Sucrose-phosphate synthase 5.2
Short name:
AtSPS5.2
UDP-glucose-fructose-phosphate glucosyltransferase
Gene namesi
Name:SPS2
Synonyms:KNS2, SPS1, SPSA2
Ordered Locus Names:At5g11110
ORF Names:T5K6.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G11110.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi596 – 5961P → L in kns2-1; pollen grain with collapsed exine structure. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10471047Probable sucrose-phosphate synthase 2PRO_0000413638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271PhosphoserineBy similarity
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei159 – 1591PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9FY54.
PRIDEiQ9FY54.

PTM databases

iPTMnetiQ9FY54.
SwissPalmiQ9FY54.

Expressioni

Tissue specificityi

Expressed in roots, cauline leaves, flower buds, flowers and anthers. Highly expressed in maturing nectaries.2 Publications

Gene expression databases

ExpressionAtlasiQ9FY54. baseline and differential.
GenevisibleiQ9FY54. AT.

Interactioni

Subunit structurei

Homodimer or homotetramer.By similarity

Protein-protein interaction databases

STRINGi3702.AT5G11110.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FY54.
SMRiQ9FY54. Positions 198-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000009685.
InParanoidiQ9FY54.
KOiK00696.
OMAiTISETHT.
PhylomeDBiQ9FY54.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR023214. HAD-like_dom.
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]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02468. sucrsPsyn_pln. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9FY54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGNDWVNSY LEAILAAEPG IANSKPPGTG DSKSSLLLRE RGHFSPTRYF
60 70 80 90 100
VEEVITGFDE TDLHRSWVQA AATRSPQERN TRLENLCWRI WNLARQKKQV
110 120 130 140 150
EGKNAKREAK REREREKARR EVTAEMSEDF SEGEKADLPG EIPTPSDNNT
160 170 180 190 200
KGRMSRISSV DVFENWFAQH KEKKLYIVLI SLHGLIRGEN MELGRDSDTG
210 220 230 240 250
GQVKYVVELA RALGSMPGVY RVDLLTRQVT APDVDSSYSE PSEMLNPIDT
260 270 280 290 300
DIEQENGESS GAYIIRIPFG PKDKYVPKEL LWPHIPEFVD RALSHIMQIS
310 320 330 340 350
KVLGEQIGGG QQVWPVSIHG HYADAGDSTA LLSGALNVPM VFTGHSLGRD
360 370 380 390 400
KLEQLLKQGR PKEEINSNYK IWRRIEAEEL CLDASEIVIT STRQEVDEQW
410 420 430 440 450
RLYDGFDPVL ERKLRARMKR GVSCLGRFMP RMVVIPPGME FHHIVPHDVD
460 470 480 490 500
ADGDDENPQT ADPPIWSEIM RFFSNPRKPM ILALARPDPK KNLVTLVKAF
510 520 530 540 550
GECRPLRELA NLTLIMGNRN DIDELSSTNS SVLLSILKLI DKYDLYGQVA
560 570 580 590 600
MPKHHQQSDV PEIYRLAAKT KGVFINPAFI EPFGLTLIEA GAHGLPTVAT
610 620 630 640 650
INGGPVDIHR VLDNGLLVDP HDQQAIADAL LKLVSDRQLW GRCRQNGLNN
660 670 680 690 700
IHLFSWPEHC KTYLARIASC KQRHPKWQRV EFENSDSDSP SDSLRDINDI
710 720 730 740 750
SLNLKLSLDG EKSGSNNGVD TNLDAEDRAA ERKAEVEKAV STLAQKSKPT
760 770 780 790 800
EKFDSKMPTL KRRKNIFVIS VDCSATSDLL AVVKTVIDAA GRGSSTGFIL
810 820 830 840 850
STSMTISETH TALLSGGLKP QDFDAVICSS GSELYFTSSG SEDKTALPYT
860 870 880 890 900
LDADYHSHIE FRWGGESLRK TLIRWISSVE EKKKTKKGEI LVEDESSSTN
910 920 930 940 950
YCLSFKVKDP ALMPPMKELR KLMRNQALRC NAVYCQNGAR LNVIPVLASR
960 970 980 990 1000
SQALRYLLVR WGIDLSNMVV FVGDSGDTDY EGLLGGIHKT VILKGLASDL
1010 1020 1030 1040
REQPGNRSYP MEDVTPLNSP NITEAKECGR DAIKVALEKL GISLLKP
Length:1,047
Mass (Da):116,966
Last modified:March 1, 2001 - v1
Checksum:i0BA67F6E8DD9FA80
GO

Sequence cautioni

The sequence AAL47425.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391222 Genomic DNA. Translation: CAC03459.1.
CP002688 Genomic DNA. Translation: AED91636.1.
AY069868 mRNA. Translation: AAL47425.1. Different initiation.
BT002697 mRNA. Translation: AAO11613.1.
PIRiT51800.
RefSeqiNP_196672.3. NM_121149.3.
UniGeneiAt.28444.

Genome annotation databases

EnsemblPlantsiAT5G11110.1; AT5G11110.1; AT5G11110.
GeneIDi830979.
GrameneiAT5G11110.1; AT5G11110.1; AT5G11110.
KEGGiath:AT5G11110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391222 Genomic DNA. Translation: CAC03459.1.
CP002688 Genomic DNA. Translation: AED91636.1.
AY069868 mRNA. Translation: AAL47425.1. Different initiation.
BT002697 mRNA. Translation: AAO11613.1.
PIRiT51800.
RefSeqiNP_196672.3. NM_121149.3.
UniGeneiAt.28444.

3D structure databases

ProteinModelPortaliQ9FY54.
SMRiQ9FY54. Positions 198-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G11110.1.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

PTM databases

iPTMnetiQ9FY54.
SwissPalmiQ9FY54.

Proteomic databases

PaxDbiQ9FY54.
PRIDEiQ9FY54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G11110.1; AT5G11110.1; AT5G11110.
GeneIDi830979.
GrameneiAT5G11110.1; AT5G11110.1; AT5G11110.
KEGGiath:AT5G11110.

Organism-specific databases

TAIRiAT5G11110.

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000009685.
InParanoidiQ9FY54.
KOiK00696.
OMAiTISETHT.
PhylomeDBiQ9FY54.

Enzyme and pathway databases

UniPathwayiUPA00371; UER00545.

Miscellaneous databases

PROiQ9FY54.

Gene expression databases

ExpressionAtlasiQ9FY54. baseline and differential.
GenevisibleiQ9FY54. AT.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR023214. HAD-like_dom.
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]
SUPFAMiSSF56784. SSF56784. 1 hit.
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] OF 149-1047 AND 154-1047.
    Strain: cv. Columbia.
  4. "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.
  5. "Identification of kaonashi mutants showing abnormal pollen exine structure in Arabidopsis thaliana."
    Suzuki T., Masaoka K., Nishi M., Nakamura K., Ishiguro S.
    Plant Cell Physiol. 49:1465-1477(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-596.
    Strain: cv. Landsberg erecta.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "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 nameiSPSA2_ARATH
AccessioniPrimary (citable) accession number: Q9FY54
Secondary accession number(s): Q8VYW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.