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31  structures 106  species 2  interactions 544  sequences 10  architectures

Family: Sucrose_synth (PF00862)

Summary: Sucrose synthase

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This is the Wikipedia entry entitled "Sucrose synthase". More...

Sucrose synthase Edit Wikipedia article

 Ribbon Diagram of Sucrose Synthase-1 3S27.
Ribbon diagram of Sucrose Synthase-1 3S27 Structure, isolated from Arabidopsis thaliana.[1]
sucrose synthase
EC number
CAS number 9030-05-1
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Sucrose synthase
Symbol Sucrose_synth
Pfam PF00862
InterPro IPR000368

In enzymology, a sucrose synthase (EC is an enzyme that catalyzes the chemical reaction

NDP-glucose + D-fructose \rightleftharpoons NDP + sucrose

Thus, the two substrates of this enzyme are NDP-glucose and D-fructose, whereas its two products are NDP and sucrose.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is NDP-glucose:D-fructose 2-alpha-D-glucosyltransferase. Other names in common use include UDPglucose-fructose glucosyltransferase, sucrose synthetase, sucrose-UDP glucosyltransferase, sucrose-uridine diphosphate glucosyltransferase, and uridine diphosphoglucose-fructose glucosyltransferase. This enzyme participates in starch and sucrose metabolism.


  1. ^ Zheng, Yi; Spencer, A.; Zhang, Y.; Garavito, R.M. (24 August 2011). "The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and its Functional Implications". Journal of Biological Chemistry. doi:10.1074/jbc.M111.275974. ; rendered with PyMOL
  • Avigad G and Milner Y (1966). "UDP-glucose:fructose transglucosylase from sugar beet roots". Methods Enzymol. 8: 341–345. doi:10.1016/0076-6879(66)08063-7. 
  • CARDINI CE, LELOIR LF, CHIRIBOGA J (1955). "The biosynthesis of sucrose". J. Biol. Chem. 214 (1): 149–55. PMID 14367373. 
  • Delmer DP (1972). "The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings". J. Biol. Chem. 247 (12): 3822–8. PMID 4624446. 
  • Murata T, Sugiyama T, Minamikawa T, Akazawa T (1966). "Enzymic mechanism of starch synthesis in ripening rice grains. 3 Mechanism of the sucrose-starch conversion". Arch. Biochem. Biophys. 113 (1): 34–44. doi:10.1016/0003-9861(66)90153-6. PMID 5941994. 
  • Yoshinaga F, Mori H, Sakai F, Hayashi T (1998). "An increase in apparent affinity for sucrose of mung bean sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11". Plant. Cell. Physiol. 39 (12): 1337–41. PMID 10050318. 
  • Porchia AC, Curatti L, Salerno GL (1999). "Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence". Planta. 210 (1): 34–40. doi:10.1007/s004250050651. PMID 10592030. 
  • Ross, HA and Davies HV (1992). "Purification and characterization of sucrose synthase from the cotyledons of Vicia fava L". Plant Physiol. 100 (2): 1008–1013. doi:10.1104/pp.100.2.1008. 
  • Silvius JE and Snyder FW (1979). "Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L". Plant Physiol. 64 (6): 1070–1073. doi:10.1104/pp.64.6.1070. 
  • Tanase K, Yamaki S (2000). "Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit". Plant. Cell. Physiol. 41 (4): 408–14. doi:10.1093/pcp/41.4.408. PMID 10845453. 
  • T, Pozueta-Romero J; Muñoz, FJ; Saikusa, T; Rodríguez-López, M; Akazawa, T; Pozueta-Romero, J (2003). "Sucrose synthase catalyzes the de novo production of ADPglucose linked to starch biosynthesis in heterotrophic tissues of plants". Plant. Cell. Physiol. 44 (5): 500–9. doi:10.1093/pcp/pcg062. PMID 12773636. 

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Sucrose synthase Provide feedback

Sucrose synthases catalyse the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family PF00534.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000368

Sucrose synthases catalyse the synthesis of sucrose EC in the following reaction: UDP-glucose + D-fructose = UDP + sucrose This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family INTERPRO. This enzyme is found mainly in plants but also appears in bacteria.

Gene Ontology

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Domain organisation

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Seed source: Pfam-B_484 (release 3.0)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 32
Number in full: 544
Average length of the domain: 389.50 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 51.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.4 19.4
Trusted cut-off 20.7 19.4
Noise cut-off 19.2 18.9
Model length: 548
Family (HMM) version: 16
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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There are 2 interactions for this family. More...

Sucrose_synth Glycos_transf_1


For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Sucrose_synth domain has been found. There are 31 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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