ID L1ILC5_GUITC Unreviewed; 648 AA.
AC L1ILC5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
GN ORFNames=GUITHDRAFT_78834 {ECO:0000313|EMBL:EKX36600.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX36600.1};
RN [1] {ECO:0000313|EMBL:EKX36600.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX36600.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX36600}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (MAR-2016) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001478};
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000256|ARBA:ARBA00004602}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily.
CC {ECO:0000256|ARBA:ARBA00010281}.
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DR EMBL; JH993071; EKX36600.1; -; Genomic_DNA.
DR RefSeq; XP_005823580.1; XM_005823523.1.
DR AlphaFoldDB; L1ILC5; -.
DR STRING; 905079.L1ILC5; -.
DR PaxDb; 55529-EKX36600; -.
DR EnsemblProtists; EKX36600; EKX36600; GUITHDRAFT_78834.
DR GeneID; 17293337; -.
DR KEGG; gtt:GUITHDRAFT_78834; -.
DR eggNOG; ENOG502QT35; Eukaryota.
DR HOGENOM; CLU_009583_18_2_1; -.
DR OMA; TWCPWYM; -.
DR OrthoDB; 2720639at2759; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
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:SF11; 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|ARBA:ARBA00023234};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000011087};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 131..382
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 445..601
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..59
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 648 AA; 72888 MW; 8D03A5E3D7191D8B CRC64;
MRRLSLRGGN DGNTGVKKNF SNERLDDAKS RLKKILGANS QLERQVADLA ASYDKLAKSY
GLGSFKPTRT ASYSCLNDVT LTEAADKAPE PEESKTPPVE SIQKKIEAAL AKDSKPVEPT
EQVLPPEERL KIVIVSSEVA PFSKSGGLAD VCDKLGVALS RMGHRVMTVA PLYWRMGVGK
DKLGNVVMTL GSVWKEFGLF KQKLRIEYFR KFRETGVDHI FVQQGCYERR GVDAGAQRHG
MYGHNDDLMR FALLSWAALE APFSVECDGS VYGDDVIFLV NDWMVGLVPL IMTSHYRRYG
CYKQARTVFD IHNMGYCGNF PVVDPHDLGL PDGAYYDKLF HDRQIKLLKG GIEMADRVVT
VSPSYRDEII TVEGGWGLQD TCRGRFPHLD GVLNGIDCDE WNPETDRFLS AKCQGYDNFF
NKDDTTGKRS CKLHLQNCMG LREDPNIPIV AFIGRLAYQK GIDVIESIFP WLMNGDHAGV
TGYVQVVMMG TGDEKYARFL RDAENHNKGR VAGFVGFTSE LEHKIIAAAD IILMPSRYEP
CGLPQMYAQR YGTVPVVHAT GGLKDSVIQY DPFQNTGTGW KFDCCDAEGL KYGLWNALNT
YKNHKDAWAG IVRRCMEQDF SWERSAKRYV EIFKWARMDP PFHQPIPF
//
