ID A0A0K9Q0C0_ZOSMR Unreviewed; 908 AA.
AC A0A0K9Q0C0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN ORFNames=ZOSMA_122G00180 {ECO:0000313|EMBL:KMZ74748.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ74748.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ74748.1}.
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DR EMBL; LFYR01000244; KMZ74748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9Q0C0; -.
DR STRING; 29655.A0A0K9Q0C0; -.
DR OMA; PLYWEIY; -.
DR OrthoDB; 141134at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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:RHEA.
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; PTHR46083; -; 1.
DR PANTHER; PTHR46083:SF2; STARCH SYNTHASE 4, CHLOROPLASTIC_AMYLOPLASTIC-RELATED; 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|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW Chloroplast {ECO:0000256|RuleBase:RU361232};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361232};
KW Plastid {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 412..652
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 704..828
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT COILED 98..188
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 237..302
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 908 AA; 104100 MW; F523C9BE1C6311C4 CRC64;
MSLFNYQLRR LQLKNDSQEK PLLKPKIQHN DEEDTIDQNA IPDCIFYSHN QTIANEDSNG
INNVSETNEV KNVNDKNQSS RIELDDLFHT INNPEKIHDN ALKELKMILV EKEMLQQKVN
ALEMKLVEDD AQTNVVHKNE IHTIETDDHE NHRIRNENMV LKSDIKMLKD KLRNVQAIDE
RVFSLENERS KLLASVKELE FMLSVAQKDV SKLSILKTEC EDLHYKIECL HALLDTATKH
ADQADRILKR NDELERKVEK LEALLKASNP DRFISDENKE CKEILLQRVK ILENQIQMSD
EKINANVPIY QGSVKELQDI VSKHKEESMG KLSNGSLDDM PQELWNHVLS MVDSWLLEKK
ISSNDAILLR EMAWKRDDRI KDAYFICNGE IQQKVIDTFL KIISSQSSSG LNIVHIAAEM
APVVKVGGLG DVVTGLCKAL QRRGHLVEVI LPKYDCMQIG EIDNLQILDV VIESYFDGHL
FKNKIWFGTI EGLPVYFIEP LHPAQFFLRG NVYGVHDDFK RFSYFSRAAL EFICQFGKKP
DIIHCHDWQT AFIPPLYWEL YAVVGFNFAK ICFTCHNFEY QGTAHASELA SCGLGIRRLH
RADRMMDNLN HDRINLVKGA IVFSNIVTTV SPTYADEVRT AQGGHGLHDT LNLHSLKFTG
IVNGIDTETW NPFTDPFLRF HYNADDLHGK DDNKDAIRKY INLSTKNPSQ PLVACITRLV
PQKGVHLIRH AIYRTLELGG QFILLGSSPI IHIQREFEDI ANQFQNHPNI RLVLKYDNAL
SHFIYAASDM FVMPSIFEPC GLTQMIAMRY GSVPIVRNTG GLNDSVFDVD DDAIPAQLKN
GFTFSKADEL GLNNALERAF HLYTSNKDGW LQLVKKNMRT DFSWNSSSVQ YEKLYLQTVA
RTTNSEFR
//
