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Database: UniProt
Entry: A0A2C9WI48_MANES
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ID   A0A2C9WI48_MANES        Unreviewed;       607 AA.
AC   A0A2C9WI48;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN   ORFNames=MANES_01G055700 {ECO:0000313|EMBL:OAY59742.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY59742.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY59742.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY59742.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727, ECO:0000256|RuleBase:RU361232}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU361232}. Plastid, amyloplast
CC       {ECO:0000256|RuleBase:RU361232}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|RuleBase:RU361232}.
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DR   EMBL; CM004387; OAY59742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9WI48; -.
DR   STRING; 3983.A0A2C9WI48; -.
DR   EnsemblPlants; OAY59742; OAY59742; MANES_01G055700.
DR   Gramene; OAY59742; OAY59742; MANES_01G055700.
DR   OMA; LGMTHPR; -.
DR   OrthoDB; 141134at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000091857; Chromosome lg1.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF3; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Amyloplast {ECO:0000256|RuleBase:RU361232};
KW   Chloroplast {ECO:0000256|RuleBase:RU361232};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361232}; Plastid {ECO:0000256|RuleBase:RU361232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU361232};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          83..342
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          399..525
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  66822 MW;  E7C7E9E5816A6F3A CRC64;
     MATATAAQFV SMSSHLSNHP SEPKANSGLM GLRSQSTTHH GLRYLNKIDK LQMRTQSKVQ
     KKVSATENVR PSGKIICGHG MNLVFVGAEV GPWSKTGGLG DVLGGLPPAL AARGHRVMTV
     SPRYDQYKDA WDTSVVVEIR VGERNETVRF FHCYKRGVDR VFVDHPLFLE KVWGKTGSKI
     YGPKAGLDYK DNQLRFSLLC LAALEAPRVL NLNSCKNFSG PYGEDVVFIA NDWHTALLPC
     YLKTFYQPSG IYRTAKVAFC IHNIAYQGRF SFSEFSQLNL PDKFRSSFDF IDGYNKPVKG
     RKINWMKAGI LESDKVLTVS PYYAQEVIDG IERGVELDNI IRKTGITGII NGMDVQEWNP
     ATDKYISINY DATTVMKAKP LLKEALQAEV GLPVGADIPL IGFIGRLEEQ KGSDILVAAI
     SQLVEHDVQI VILGTGKSSF ETQIEQLEVQ YPDKARGLAK FNVTLAHMII AGSDFMLIPS
     RFEPCGLIQL HAMRYGTIPI VASTGGLVDT VKEGYTGFHI GAFNVDCETI DPADVAAVVK
     TVGRAIATYT TSSLREMILN CMAQDFSWKG PARLWEKLLL SLEVADSEAG IEGEEITPLA
     MENVPAP
//
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