SSY3_SOLTU
ID SSY3_SOLTU Reviewed; 1230 AA.
AC Q43846; O04842;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Soluble starch synthase 3, chloroplastic/amyloplastic;
DE EC=2.4.1.21;
DE AltName: Full=Soluble starch synthase III;
DE Short=SS III;
DE Flags: Precursor;
GN Name=SS3; Synonyms=SSIII;
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], AND PROTEIN SEQUENCE OF 767-773 AND 1000-1014.
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RX PubMed=8768372; DOI=10.2307/3870356;
RA Marshall J., Sidebottom C., Debet M., Martin C., Smith A.M., Edwards A.;
RT "Identification of the major starch synthase in the soluble fraction of
RT potato tubers.";
RL Plant Cell 8:1121-1135(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Desiree;
RX PubMed=9011082; DOI=10.1046/j.1365-313x.1996.10060981.x;
RA Abel G.J.W., Springer F., Willmitzer L., Kossmann J.;
RT "Cloning and functional analysis of a cDNA encoding a novel 139 kDa starch
RT synthase from potato (Solanum tuberosum L.).";
RL Plant J. 10:981-991(1996).
CC -!- FUNCTION: May account for most of the soluble starch synthase activity
CC in the tubers. Contributes only a tiny percentage of the granule-bound
CC activity, but may also contribute to the deposition of transient starch
CC in chloroplasts of leaves.
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 -!- TISSUE SPECIFICITY: Tuber, sink and source leaves.
CC -!- INDUCTION: By sucrose under illumination.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR EMBL; X95759; CAA65065.1; -; mRNA.
DR EMBL; X94400; CAA64173.1; -; mRNA.
DR PIR; T07663; T07663.
DR AlphaFoldDB; Q43846; -.
DR SMR; Q43846; -.
DR STRING; 4113.PGSC0003DMT400042496; -.
DR CAZy; CBM53; Carbohydrate-Binding Module Family 53.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PRIDE; Q43846; -.
DR InParanoid; Q43846; -.
DR BioCyc; MetaCyc:MON-1884; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43846; baseline.
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:2001070; F:starch binding; 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 Gene3D; 2.60.40.10; -; 2.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF16760; CBM53; 3.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SMART; SM01066; CBM_25; 3.
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..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..1230
FT /note="Soluble starch synthase 3,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000011146"
FT REGION 66..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 794
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="S -> P (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="I -> F (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..59
FT /note="SI -> PF (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="F -> L (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="P -> T (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="K -> Q (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="G -> V (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="N -> D (in Ref. 2; CAA64173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1230 AA; 139111 MW; 3D95524F3DD9349E CRC64;
MDVPFPLHRS LSCTSVSNAI THLKIKPILG FVSHGTTSLS VQSSSWRKDG MVTGVSFSIC
ANFSGRRRRK VSTPRSQGSS PKGFVPRKPS GMSTQRKVQK SNGDKESKST STSKESEISN
QKTVEARVET SDDDTKGVVR DHKFLEDEDE INGSTKSISM SPVRVSSQFV ESEETGGDDK
DAVKLNKSKR SEESGFIIDS VIREQSGSQG ETNASSKGSH AVGTKLYEIL QVDVEPQQLK
ENNAGNVEYK GPVASKLLEI TKASDVEHTE SNEIDDLDTN SFFKSDLIEE DEPLAAGTVE
TGDSSLNLRL EMEANLRRQA IERLAEENLL QGIRLFCFPE VVKPDEDVEI FLNRGLSTLK
NESDVLIMGA FNEWRYRSFT TRLTETHLNG DWWSCKIHVP KEAYRADFVF FNGQDVYDNN
DGNDFSITVK GGMQIIDFEN FLLEEKWREQ EKLAKEQAER ERLAEEQRRI EAEKAEIEAD
RAQAKEEAAK KKKVLRELMV KATKTRDITW YIEPSEFKCE DKVRLYYNKS SGPLSHAKDL
WIHGGYNNWK DGLSIVKKLV KSERIDGDWW YTEVVIPDQA LFLDWVFADG PPKHAIAYDN
NHRQDFHAIV PNHIPEELYW VEEEHQIFKT LQEERRLREA AMRAKVEKTA LLKTETKERT
MKSFLLSQKH VVYTEPLDIQ AGSSVTVYYN PANTVLNGKP EIWFRCSFNR WTHRLGPLPP
QKMSPAENGT HVRATVKVPL DAYMMDFVFS EREDGGIFDN KSGMDYHIPV FGGVAKEPPM
HIVHIAVEMA PIAKVGGLGD VVTSLSRAVQ DLNHNVDIIL PKYDCLKMNN VKDFRFHKNY
FWGGTEIKVW FGKVEGLSVY FLEPQNGLFS KGCVYGCSND GERFGFFCHA ALEFLLQGGF
SPDIIHCHDW SSAPVAWLFK EQYTHYGLSK SRIVFTIHNL EFGADLIGRA MTNADKATTV
SPTYSQEVSG NPVIAPHLHK FHGIVNGIDP DIWDPLNDKF IPIPYTSENV VEGKTAAKEA
LQRKLGLKQA DLPLVGIITR LTHQKGIHLI KHAIWRTLER NGQVVLLGSA PDPRVQNNFV
NLANQLHSKY NDRARLCLTY DEPLSHLIYA GADFILVPSI FEPCGLTQLT AMRYGSIPVV
RKTGGLYDTV FDVDHDKERA QQCGLEPNGF SFDGADAGGV DYALNRALSA WYDGRDWFNS
LCKQVMEQDW SWNRPALDYL ELYHAARKLE
