SSY2_SOLTU
ID SSY2_SOLTU Reviewed; 767 AA.
AC Q43847;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Granule-bound starch synthase 2, chloroplastic/amyloplastic;
DE EC=2.4.1.21;
DE AltName: Full=Granule-bound starch synthase II;
DE Short=GBSS-II;
DE Short=SS II;
DE Flags: Precursor;
GN Name=SS2; Synonyms=SSII;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-55, AND VARIANT ASP-51.
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RX PubMed=7670507; DOI=10.1046/j.1365-313x.1995.08020283.x;
RA Edwards A., Marshall J., Sidebottom C., Visser R.G.F., Smith A.M.,
RA Martin C.;
RT "Biochemical and molecular characterization of a novel starch synthase from
RT potato tubers.";
RL Plant J. 8:283-294(1995).
RN [2]
RP SEQUENCE REVISION.
RA Shearer N., Edwards E.A., Martin C., Bornemann S.;
RT "Resequencing, expression and purification of His-tagged potato soluble
RT starch synthase II in Escherichia coli.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [4]
RP FUNCTION.
RX PubMed=10420646; DOI=10.1007/s004250050587;
RA Kossmann J., Abel G.J.W., Springer F., Lloyd J.R., Willmitzer L.;
RT "Cloning and functional analysis of a cDNA encoding a starch synthase from
RT potato (Solanum tuberosum L.) that is predominantly expressed in leaf
RT tissue.";
RL Planta 208:503-511(1999).
CC -!- FUNCTION: Accounts for only 10 to 15% of the total soluble starch
CC synthase activity in tubers. {ECO:0000269|PubMed:10420646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Plastid,
CC amyloplast {ECO:0000250}. Note=Amyloplast or chloroplast, granule-bound
CC and soluble. {ECO:0000250}.
CC -!- INDUCTION: Constant expression in light and darkness.
CC -!- MISCELLANEOUS: May be the main starch synthase responsible for the
CC incorporation of phosphorylated precursors into growing alpha-1,4-
CC glucans.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR EMBL; X87988; CAA61241.2; -; mRNA.
DR PIR; T07667; T07667.
DR RefSeq; NP_001274977.1; NM_001288048.1.
DR AlphaFoldDB; Q43847; -.
DR SMR; Q43847; -.
DR STRING; 4113.PGSC0003DMT400003356; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR EnsemblPlants; PGSC0003DMT400003356; PGSC0003DMT400003356; PGSC0003DMG400001328.
DR GeneID; 102583115; -.
DR Gramene; PGSC0003DMT400003356; PGSC0003DMT400003356; PGSC0003DMG400001328.
DR KEGG; sot:102583115; -.
DR eggNOG; ENOG502QT35; Eukaryota.
DR HOGENOM; CLU_009583_31_1_1; -.
DR InParanoid; Q43847; -.
DR OMA; RFPFFTH; -.
DR OrthoDB; 732319at2759; -.
DR SABIO-RK; Q43847; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43847; baseline and differential.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
PE 1: Evidence at protein level;
KW Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7670507"
FT CHAIN 46..767
FT /note="Granule-bound starch synthase 2,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000011145"
FT REGION 160..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT VARIANT 51
FT /note="S -> D"
FT /evidence="ECO:0000269|PubMed:7670507"
SQ SEQUENCE 767 AA; 85222 MW; 7C6405995FEC996B CRC64;
MENSILLHSG NQFHPNLPLL ALRPKKLSLI HGSSREQMWR IKRVKATGEN SGEAASADES
NDALQVTIEK SKKVLAMQQD LLQQIAERRK VVSSIKSSLA NAKGTYDGGS GSLSDVDIPD
VDKDYNVTVP STAATPITDV DKNTPPAISQ DFVESKREIK RDLADERAPP LSRSSITASS
QISSTVSSKR TLNVPPETPK SSQETLLDVN SRKSLVDVPG KKIQSYMPSL RKESSASHVE
QRNENLEGSS AEANEETEDP VNIDEKPPPL AGTNVMNIIL VASECAPWSK TGGLGDVAGA
LPKALARRGH RVMVVAPRYD NYPEPQDSGV RKIYKVDGQD VEVTYFQAFI DGVDFVFIDS
HMFRHIGNNI YGGNRVDILK RMVLFCKAAI EVPWHVPCGG VCYGDGNLVF IANDWHTALL
PVYLKAYYRD NGIMNYTRSV LVIHNIAHQG RGPLEDFSYV DLPPHYMDPF KLYDPVGGEH
FNIFAAGLKT ADRVVTVSHG YSWELKTSQG GWGLHQIINE NDWKLQGIVN GIDTKEWNPE
LDVHLQSDGY MNYSLDTLQT GKPQCKAALQ KELGLPVRDD VPLIGFIGRL DPQKGVDLIA
EAVPWMMGQD VQLVMLGTGR RDLEQMLRQF ECQHNDKIRG WVGFSVKTSH RITAGADILL
MPSRFEPCGL NQLYAMKYGT IPVVHAVGGL RDTVQPFDPF NESGLGWTFS RAEASQLIHA
LGNCLLTYRE YKKSWEGIQT RCMTQDLSWD NAAQNYEEVL IAAKYQW
