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Q43847 (SSY2_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Granule-bound starch synthase 2, chloroplastic/amyloplastic

EC=2.4.1.21
Alternative name(s):
Granule-bound starch synthase II
Short name=GBSS-II
Short name=SS II
Gene names
Name:SS2
Synonyms:SSII
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accounts for only 10 to 15% of the total soluble starch synthase activity in tubers. Ref.4

Catalytic activity

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1). HAMAP-Rule MF_00484

Pathway

Glycan biosynthesis; starch biosynthesis. HAMAP-Rule MF_00484

Subcellular location

Plastidchloroplast By similarity. Plastidamyloplast By similarity. Note: Amyloplast or chloroplast, granule-bound and soluble By similarity. HAMAP-Rule MF_00484

Induction

Constant expression in light and darkness. HAMAP-Rule MF_00484

Miscellaneous

May be the main starch synthase responsible for the incorporation of phosphorylated precursors into growing alpha-1,4-glucans.

Sequence similarities

Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.

Ontologies

Keywords
   Biological processStarch biosynthesis
   Cellular componentAmyloplast
Chloroplast
Plastid
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamylopectin biosynthetic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

starch biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionstarch synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Chloroplast Ref.1
Chain46 – 767722Granule-bound starch synthase 2, chloroplastic/amyloplastic HAMAP-Rule MF_00484
PRO_0000011145

Sites

Binding site2901ADP-glucose By similarity

Natural variations

Natural variant511S → D. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q43847 [UniParc].

Last modified January 4, 2005. Version 3.
Checksum: 7C6405995FEC996B

FASTA76785,222
        10         20         30         40         50         60 
MENSILLHSG NQFHPNLPLL ALRPKKLSLI HGSSREQMWR IKRVKATGEN SGEAASADES 

        70         80         90        100        110        120 
NDALQVTIEK SKKVLAMQQD LLQQIAERRK VVSSIKSSLA NAKGTYDGGS GSLSDVDIPD 

       130        140        150        160        170        180 
VDKDYNVTVP STAATPITDV DKNTPPAISQ DFVESKREIK RDLADERAPP LSRSSITASS 

       190        200        210        220        230        240 
QISSTVSSKR TLNVPPETPK SSQETLLDVN SRKSLVDVPG KKIQSYMPSL RKESSASHVE 

       250        260        270        280        290        300 
QRNENLEGSS AEANEETEDP VNIDEKPPPL AGTNVMNIIL VASECAPWSK TGGLGDVAGA 

       310        320        330        340        350        360 
LPKALARRGH RVMVVAPRYD NYPEPQDSGV RKIYKVDGQD VEVTYFQAFI DGVDFVFIDS 

       370        380        390        400        410        420 
HMFRHIGNNI YGGNRVDILK RMVLFCKAAI EVPWHVPCGG VCYGDGNLVF IANDWHTALL 

       430        440        450        460        470        480 
PVYLKAYYRD NGIMNYTRSV LVIHNIAHQG RGPLEDFSYV DLPPHYMDPF KLYDPVGGEH 

       490        500        510        520        530        540 
FNIFAAGLKT ADRVVTVSHG YSWELKTSQG GWGLHQIINE NDWKLQGIVN GIDTKEWNPE 

       550        560        570        580        590        600 
LDVHLQSDGY MNYSLDTLQT GKPQCKAALQ KELGLPVRDD VPLIGFIGRL DPQKGVDLIA 

       610        620        630        640        650        660 
EAVPWMMGQD VQLVMLGTGR RDLEQMLRQF ECQHNDKIRG WVGFSVKTSH RITAGADILL 

       670        680        690        700        710        720 
MPSRFEPCGL NQLYAMKYGT IPVVHAVGGL RDTVQPFDPF NESGLGWTFS RAEASQLIHA 

       730        740        750        760 
LGNCLLTYRE YKKSWEGIQT RCMTQDLSWD NAAQNYEEVL IAAKYQW 

« Hide

References

« Hide 'large scale' references
[1]"Biochemical and molecular characterization of a novel starch synthase from potato tubers."
Edwards A., Marshall J., Sidebottom C., Visser R.G.F., Smith A.M., Martin C.
Plant J. 8:283-294(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-55, VARIANT ASP-51.
Strain: cv. Desiree.
Tissue: Tuber.
[2]"Resequencing, expression and purification of His-tagged potato soluble starch synthase II in Escherichia coli."
Shearer N., Edwards E.A., Martin C., Bornemann S.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Genome sequence and analysis of the tuber crop potato."
The Potato Genome Sequencing Consortium
Nature 475:189-195(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. DM1-3 516 R44.
[4]"Cloning and functional analysis of a cDNA encoding a starch synthase from potato (Solanum tuberosum L.) that is predominantly expressed in leaf tissue."
Kossmann J., Abel G.J.W., Springer F., Lloyd J.R., Willmitzer L.
Planta 208:503-511(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87988 mRNA. Translation: CAA61241.2.
PIRT07667.
RefSeqNP_001274977.1. NM_001288048.1.
UniGeneStu.662.

3D structure databases

ProteinModelPortalQ43847.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT5. Glycosyltransferase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsPGSC0003DMT400003356; PGSC0003DMT400003356; PGSC0003DMG400001328.
GeneID102583115.
KEGGsot:102583115.

Phylogenomic databases

KOK00703.

Enzyme and pathway databases

UniPathwayUPA00152.

Family and domain databases

HAMAPMF_00484. Glycogen_synth.
InterProIPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR02095. glgA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSSY2_SOLTU
AccessionPrimary (citable) accession number: Q43847
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways