ID A0A2J6LMW0_LACSA Unreviewed; 993 AA.
AC A0A2J6LMW0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-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=LSAT_7X34440 {ECO:0000313|EMBL:PLY88665.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY88665.1};
RN [1] {ECO:0000313|EMBL:PLY88665.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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:PLY88665.1}.
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DR EMBL; NBSK01002986; PLY88665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LMW0; -.
DR STRING; 4236.A0A2J6LMW0; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_7X34440_mrna; cds-PLY88665.1; gene-LSAT_7X34440.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_7X34440_mrna; cds-PLY88665.1; gene-LSAT_7X34440.
DR OrthoDB; 141134at2759; -.
DR UniPathway; UPA00152; -.
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|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}; Plastid {ECO:0000256|RuleBase:RU361232};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 494..734
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 788..943
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 63..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..191
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 227..285
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 327..410
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 993 AA; 113038 MW; 4BDCC1349256CDCA CRC64;
MAGKLSTCFL SHQWSCCTVL DCKHLNVRFY SLPSPRFATV SCKIRQRNSS LPPRRPQAKK
IIPAQIPQND NLMTPGNENS DSENEDDFSH QSTSDEVVAI QRFDDKNSSS KLIPSIGADK
VGEVTTVNLQ DVIGMIRNAE KNIHILNQAR INAIEDLETI LSEKEVLQRE INNLEMRLAE
TDARIRVAAQ DKIHVELLQD HLEKLQSEMS NNGAHDAVVL RSPDRQTRAL SEELNSLRNE
NMSLQNDLNT LKEQLRDVKR TDERVEMLEN ERTVLELSIK ELEYKLTVSQ QDGVQLSTLR
SECETLWNKV EHLQGLLDKS TSQADQAILV LQQNQELRKK VERLEESLED ANIYKLSSEK
LQQYNDLMQQ KIKLLDERLE RSDAEIHSYV QLYQDSVKEF QETLDNLKEE SKKKASGKQV
DMPWEFWSRL LLMFDAWFLE KKIHGDEAKL LREMTWKKDG RIHDVYIECK EKNEREIIAA
FRRLTSSSSG SGLHVVHIAA EMAPVAKVGG LGDVLSALSK ALQKKGHLVE IILPKYDCMQ
YESIQNLRVL DLAVESYFDG HLFKNKIWIG TVEGLPVYFI EPLHPAKFFW RGKTYGEPDD
LKRFSFFSRA ALELLHQSGK KPDIIHCHDW QTAFVAPLYW DLYAPKGLNS ARICFTCHNF
EYQGTASASE IASCGLDIHH LNRPDRMQDN SSHDRLNPVK GAIVFSNIVT TVSPTYAQEV
RTSQGGQGLH ATLNAHSQKF VGILNGIDTD SWNPATDTYL SFQYNSSDLE GKSENKNALR
RHLGLSLSDS RRPLVGCITR LVPQKGVHLI RHAIYRALEL GGQFVLLGSS PVPNIHREFE
EIAKKFQTHE HIRLILKYDE ALSHSIYAAS DMFIIPSIFE PCGLTQMIAM RYGAIPVARK
TGGLNDSVFD VDDDTIPIQL RNGFTFVTPD EHAFNGAFDR AFKYYKNDSE GWEELMKKVM
NIDFSWDTSA SQYEELYLQS VSKAKAARRA AAG
//
