Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sucrose-phosphate synthase

Gene

SPS1

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

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.

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. Sucrose-phosphate synthase (SPS1)
  2. no protein annotated in this organism
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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-1742.
BRENDAi2.4.1.14. 5812.
UniPathwayiUPA00371; UER00545.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrose-phosphate synthase (EC:2.4.1.14)
Alternative name(s):
UDP-glucose-fructose-phosphate glucosyltransferase
Gene namesi
Name:SPS1
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10561056Sucrose-phosphate synthasePRO_0000204674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei158 – 1581Phosphoserine2 Publications
Modified residuei424 – 4241Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Ser-158 and Ser-424.2 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiP31928.

Interactioni

Subunit structurei

Homodimer or homotetramer.By similarity

Protein-protein interaction databases

IntActiP31928. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP31928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 1 family.Curated

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.

P31928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNDWINSY LEAILDVGGQ GIDASTGKTS TAPPSLLLRE RGHFSPSRYF
60 70 80 90 100
VEEVISGFDE TDLHRSWVRA ASTRSPQERN TRLENLCWRI WNLARKKKQI
110 120 130 140 150
EGEEAQRLAK RHVERERGRR EATADMSEDL SEGERGDTVA DMLFASESTK
160 170 180 190 200
GRMRRISSVE MMDNWANTFK EKKLYVVLIS LHGLIRGENM ELGRDSDTGG
210 220 230 240 250
QVKYVVELAR ALGSMPGVYR VDLLTRQVSA PGVDWSYGEP TEMLSSRNSE
260 270 280 290 300
NSTEQLGESS GAYIIRIPFG PKDKYVAKEL LWPYIPEFVD GALSHIKQMS
310 320 330 340 350
KVLGEQIGGG LPVWPASVHG HYADAGDSAA LLSGALNVPM VFTGHSLGRD
360 370 380 390 400
KLDQLLKQGR LSREEVDATY KIMRRIEAEE LCLDASEIVI TSTRQEIEEQ
410 420 430 440 450
WQLYHGFDLV LERKLRARMR RGVSCHGRFM PRMAKIPPGM EFNHIAPEDA
460 470 480 490 500
DMDTDIDGHK ESNANPDPVI WSEIMRFFSN GRKPMILALA RPDPKKNLTT
510 520 530 540 550
LVKAFGECRP LRELANLTLI IGNRDDIDEM STTSSSVLIS ILKLIDKYDL
560 570 580 590 600
YGQVAYPKHH KQSDVPDIYR LAAKTKGVFI NPAFIEPFGL TLIEAAAYGL
610 620 630 640 650
PIVATKNGGP VDIIGVLDNG LLIDPHDQKS IADALLKLVA DKHLWTKCRQ
660 670 680 690 700
NGLKNIHLFS WPEHCKNYLS RIASCKPRQP NWQRIDEGSE NSDTDSAGDS
710 720 730 740 750
LRDIQDISLN LKLSLDAERT EGGNSFDDSL DSEEANAKRK IENAVAKLSK
760 770 780 790 800
SMDKAQVDVG NLKFPAIRRR KCIFVIALDC DVTSDLLQVI KTVISIVGEQ
810 820 830 840 850
RPTGSIGFIL STSMTLSEVD SLLDSGGLRP ADFDAFICNS GSELYYPSTD
860 870 880 890 900
YSESPFVLDQ DYYSHIDYRW GGEGLWKTLV KWAASVNEKK GENAPNIVIA
910 920 930 940 950
DETSSTTHCY AFKVNDFTLA PPAKELRKMM RIQALRCHAI YCQNGTRLNV
960 970 980 990 1000
IPVLASRSQA LRYLFMRWGV ELSNFVVFVG ESGDTDYEGL LGGVHKTVIL
1010 1020 1030 1040 1050
KGIGSNTSNF HATRAYPMEH VMPVDSPNMF QTGGCNIDDI SDALSKIGCL

KAQKSL
Length:1,056
Mass (Da):117,716
Last modified:July 1, 1993 - v1
Checksum:i7443A1FD3F1AB336
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171V → I in AAC60545 (PubMed:7763376).Curated
Sequence conflicti69 – 757RAASTRS → ALHQLAG in AAC60545 (PubMed:7763376).Curated
Sequence conflicti604 – 6041A → R in AAC60545 (PubMed:7763376).Curated
Sequence conflicti643 – 6442HL → QV in AAC60545 (PubMed:7763376).Curated
Sequence conflicti947 – 9471R → W in AAC60545 (PubMed:7763376).Curated
Sequence conflicti1038 – 10392DD → EH in AAC60545 (PubMed:7763376).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04803 mRNA. Translation: AAA20092.1.
S54379 mRNA. Translation: AAC60545.2.
PIRiJQ2277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04803 mRNA. Translation: AAA20092.1.
S54379 mRNA. Translation: AAC60545.2.
PIRiJQ2277.

3D structure databases

ProteinModelPortaliP31928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP31928. 1 interaction.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

PTM databases

iPTMnetiP31928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00371; UER00545.
BioCyciMetaCyc:MONOMER-1742.
BRENDAi2.4.1.14. 5812.

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

  1. "Identification of the uridine-binding domain of sucrose-phosphate synthase. Expression of a region of the protein that photoaffinity labels with 5-azidouridine diphosphate-glucose."
    Salvucci M.E., Klein R.R.
    Plant Physiol. 102:529-536(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Purification, cloning and expression of spinach leaf sucrose-phosphate synthase in Escherichia coli."
    Sonnewald U., Quick W.P., Macrae E., Krause K.P., Stitt M.
    Planta 189:174-181(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.
  3. "Identification of the major regulatory phosphorylation site in sucrose-phosphate synthase."
    McMichael R.W. Jr., Klein R.R., Salvucci M.E., Huber S.C.
    Arch. Biochem. Biophys. 307:248-252(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 156-170, PHOSPHORYLATION AT SER-158.
  4. "Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves."
    Toroser D., Huber S.C.
    Plant Physiol. 114:947-955(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-158 AND SER-424.

Entry informationi

Entry nameiSPSA_SPIOL
AccessioniPrimary (citable) accession number: P31928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 6, 2016
This is version 86 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.