ID O64927_CHLRE Unreviewed; 651 AA.
AC O64927;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 2.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN ORFNames=CHLRE_16g665800v5 {ECO:0000313|EMBL:PNW71709.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:AAC17971.2};
RN [1] {ECO:0000313|EMBL:AAC17971.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=137C {ECO:0000313|EMBL:AAC17971.2};
RA D'hulst C., Abel G., Kossmann J., Ball S.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAC17971.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=137C {ECO:0000313|EMBL:AAC17971.2};
RA Wattebled F., Ral J.-P., Gao M., Abel G.J., Wattebled-Bernege A.-G.,
RA Kossman J., Myers A.M., Chibbar R.N., Ball S.G., D'Hulst C.;
RT "Cloning of a cDNA encoding for a soluble starch synthase isoform in the
RT green alga Chlamydomonas reinhardtii.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAC17971.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=137C {ECO:0000313|EMBL:AAC17971.2};
RA Wattebled F., Ral J.-P., Gao M., Abel G.J., Wattebled-Bernege A.-G.,
RA Kossmann J., Myers A.M., Chibbar R.N., Ball S.G., D'Hulst C.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PNW71709.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+
RC {ECO:0000313|EMBL:PNW71709.1};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [5] {ECO:0000313|EMBL:PNW71709.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW71709.1};
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) 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; AF026422; AAC17971.2; -; mRNA.
DR EMBL; CM008977; PNW71709.1; -; Genomic_DNA.
DR PIR; T07926; T07926.
DR RefSeq; XP_001701469.1; XM_001701417.1.
DR STRING; 3055.O64927; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; 3055-EDO97466; -.
DR EnsemblPlants; PNW71709; PNW71709; CHLRE_16g665800v5.
DR GeneID; 5727013; -.
DR Gramene; PNW71709; PNW71709; CHLRE_16g665800v5.
DR KEGG; cre:CHLRE_16g665800v5; -.
DR eggNOG; ENOG502QPHZ; Eukaryota.
DR HOGENOM; CLU_009583_18_3_1; -.
DR OMA; HNEAFKG; -.
DR OrthoDB; 530172at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000006906; Chromosome 16.
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; PTHR46083; -; 1.
DR PANTHER; PTHR46083:SF1; GLYCOGEN SYNTHASE 2-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 2: Evidence at transcript level;
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 Reference proteome {ECO:0000313|Proteomes:UP000006906};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAC17971.2}.
FT DOMAIN 149..392
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 459..617
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT COILED 48..75
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 71155 MW; 9BC2BC331B8F444C CRC64;
MKSFMRRDAL GAGLRGAAST KPVSRVASVR PAPTAYRTAC QVAKVDEMVS VDEELTRLRK
ENELLRAQLA LYQQNQQPSV GAAAVAPPAA ATKVLEKPAP AKQASVDGGI IWPKPGEAFW
ERSPRASPMP LQGGAAEAPP VERDGNPMHI IHITAEMAPI AKVGGLGDVV TGLAKAALAR
GHFVTVMLPF YECLPKDQIE GLKHECDIEV PKGYRWDGEI RVGPLKTSVF WGRVQGCPVY
LIKPADDTNC NIFRGGRIYG GSYNEMEAYL YFCRACLEYL NVSQQNPHVL QLHDWHAAAA
SMLYWDVYNP NGFSRTRLML TIHNLDNTGE TRQDEFFFTG VPGENFATID KALDERTIGH
NPERLNLMKG GIVYCNAVTT VSPTYANEVL NGGAAGWLRS TFARPELRSK FHGILNGIDC
EEWNPATDAL LPANFDADRP AGKALCKEFL QKGLGLEVDP RKPLVAVVSR LVPQKGIHLI
KAALFRTVEK GGQFVLLGSG HSDPAFRQLA DGQFKDHPNC RLKIMYSERL AHMIYAAADV
VVVPSMFEPC GLTQMIALRY GAVPLVRRTG GLADTVFDVD GPAGGPAQPR NGFVFDGSDD
GALHGALDRA LTLYTTQPER WAALQQDNMR LDVSWGKSAK SYVDVYRSIS A
//
