SSG1_ARATH
ID SSG1_ARATH Reviewed; 610 AA.
AC Q9MAQ0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Granule-bound starch synthase 1, chloroplastic/amyloplastic {ECO:0000303|PubMed:15347792};
DE Short=AtGBS1 {ECO:0000303|PubMed:15347792};
DE Short=AtGBSS1 {ECO:0000303|PubMed:12777053};
DE EC=2.4.1.242 {ECO:0000250|UniProtKB:P84633};
DE AltName: Full=Granule-bound starch synthase I;
DE Short=GBSS-I;
DE Flags: Precursor;
GN Name=GBSS1 {ECO:0000303|PubMed:12777053};
GN Synonyms=GBS1 {ECO:0000303|PubMed:15347792},
GN GBSS {ECO:0000303|PubMed:25710501}, WAXY;
GN OrderedLocusNames=At1g32900 {ECO:0000312|Araport:AT1G32900};
GN ORFNames=F9L11.8 {ECO:0000312|EMBL:AAF31273.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INDUCTION BY LIGHT, AND TISSUE SPECIFICITY.
RX PubMed=12777053; DOI=10.1023/a:1023053420632;
RA Tenorio G., Orea A., Romero J.M., Merida A.;
RT "Oscillation of mRNA level and activity of granule-bound starch synthase I
RT in Arabidopsis leaves during the day/night cycle.";
RL Plant Mol. Biol. 51:949-958(2003).
RN [6]
RP FUNCTION, INDUCTION BY LIGHT, AND SUBCELLULAR LOCATION.
RX PubMed=15347792; DOI=10.1104/pp.104.044347;
RA Smith S.M., Fulton D.C., Chia T., Thorneycroft D., Chapple A., Dunstan H.,
RA Hylton C., Zeeman S.C., Smith A.M.;
RT "Diurnal changes in the transcriptome encoding enzymes of starch metabolism
RT provide evidence for both transcriptional and posttranscriptional
RT regulation of starch metabolism in Arabidopsis leaves.";
RL Plant Physiol. 136:2687-2699(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, 3D-STRUCTURE
RP MODELING, MUTAGENESIS OF LYS-441; GLU-449; GLU-452 AND GLU-486, AND
RP INTERACTION WITH PTST.
RC STRAIN=cv. Columbia;
RX PubMed=25710501; DOI=10.1371/journal.pbio.1002080;
RA Seung D., Soyk S., Coiro M., Maier B.A., Eicke S., Zeeman S.C.;
RT "PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND
RT STARCH SYNTHASE to starch granules and for normal amylose synthesis in
RT Arabidopsis.";
RL PLoS Biol. 13:E1002080-E1002080(2015).
CC -!- FUNCTION: Required for the synthesis of amylose (PubMed:25710501).
CC Destroyed as it is released from the starch granules during the night
CC (PubMed:15347792). The circadian expression is controlled by CCA1 and
CC LHY transcription factors (PubMed:12777053).
CC {ECO:0000269|PubMed:12777053, ECO:0000269|PubMed:15347792,
CC ECO:0000269|PubMed:25710501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose =
CC [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate +
CC H(+); Xref=Rhea:RHEA:15873, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:76533; EC=2.4.1.242;
CC Evidence={ECO:0000250|UniProtKB:P84633};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Interacts with PTST. This interaction is critical for the
CC localization to starch granules. {ECO:0000269|PubMed:25710501}.
CC -!- INTERACTION:
CC Q9MAQ0; Q94AX2: PTST; NbExp=2; IntAct=EBI-2355339, EBI-4430187;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15347792, ECO:0000269|PubMed:25710501}.
CC Note=Exclusively bound to starch granules and found in the soluble
CC fraction only if PTST is absent. {ECO:0000269|PubMed:15347792,
CC ECO:0000269|PubMed:25710501}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, flowers, fruits
CC and at much higher levels in leaves. {ECO:0000269|PubMed:12777053}.
CC -!- INDUCTION: Circadian-regulation. Strong up-regulation at the end of the
CC night and the beginning of the light period.
CC {ECO:0000269|PubMed:12777053, ECO:0000269|PubMed:15347792}.
CC -!- DISRUPTION PHENOTYPE: Production of amylose-free starch.
CC {ECO:0000269|PubMed:25710501}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR EMBL; AC006424; AAF31273.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31537.1; -; Genomic_DNA.
DR EMBL; AY094405; AAM19783.1; -; mRNA.
DR EMBL; AY123983; AAM74496.1; -; mRNA.
DR EMBL; AY149948; AAN31102.1; -; mRNA.
DR EMBL; AY088544; AAM66076.1; -; mRNA.
DR PIR; F86453; F86453.
DR RefSeq; NP_174566.1; NM_103023.4.
DR AlphaFoldDB; Q9MAQ0; -.
DR SMR; Q9MAQ0; -.
DR BioGRID; 25418; 2.
DR DIP; DIP-53368N; -.
DR IntAct; Q9MAQ0; 2.
DR STRING; 3702.AT1G32900.1; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q9MAQ0; -.
DR PRIDE; Q9MAQ0; -.
DR ProteomicsDB; 228326; -.
DR EnsemblPlants; AT1G32900.1; AT1G32900.1; AT1G32900.
DR GeneID; 840184; -.
DR Gramene; AT1G32900.1; AT1G32900.1; AT1G32900.
DR KEGG; ath:AT1G32900; -.
DR Araport; AT1G32900; -.
DR TAIR; locus:2037950; AT1G32900.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR HOGENOM; CLU_009583_18_2_1; -.
DR InParanoid; Q9MAQ0; -.
DR OMA; CGWVHGR; -.
DR OrthoDB; 1142473at2759; -.
DR PhylomeDB; Q9MAQ0; -.
DR BioCyc; ARA:AT1G32900-MON; -.
DR BRENDA; 2.4.1.242; 399.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q9MAQ0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAQ0; baseline and differential.
DR Genevisible; Q9MAQ0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009569; C:chloroplast starch grain; IDA:TAIR.
DR GO; GO:0102502; F:ADP-glucose-starch glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Glycosyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..610
FT /note="Granule-bound starch synthase 1,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000011125"
FT COILED 438..454
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250|UniProtKB:P0A6U8"
FT MUTAGEN 441
FT /note="K->E: No effect on activity, but reduced interaction
FT with PTST."
FT /evidence="ECO:0000269|PubMed:25710501"
FT MUTAGEN 449
FT /note="E->K: No effect on activity, but reduced interaction
FT with PTST."
FT /evidence="ECO:0000269|PubMed:25710501"
FT MUTAGEN 452
FT /note="E->K: No effect on activity, but loss of interaction
FT with PTST."
FT /evidence="ECO:0000269|PubMed:25710501"
FT MUTAGEN 486
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25710501"
SQ SEQUENCE 610 AA; 66879 MW; CF17F25BE12220DF CRC64;
MATVTASSNF VSRTSLFNNH GASSCSDVAQ ITLKGQSLTH CGLRSFNMVD NLQRRSQAKP
VSAKSSKRSS KVKTAGKIVC EKGMSVIFIG AEVGPWSKTG GLGDVLGGLP PALAARGHRV
MTICPRYDQY KDAWDTCVVV QIKVGDKVEN VRFFHCYKRG VDRVFVDHPI FLAKVVGKTG
SKIYGPITGV DYNDNQLRFS LLCQAALEAP QVLNLNSSKY FSGPYGEDVV FVANDWHTAL
LPCYLKSMYQ SRGVYMNAKV VFCIHNIAYQ GRFAFDDYSL LNLPISFKSS FDFMDGYEKP
VKGRKINWMK AAILEAHRVL TVSPYYAQEL ISGVDRGVEL HKYLRMKTVS GIINGMDVQE
WNPSTDKYID IKYDITTVTD AKPLIKEALQ AAVGLPVDRD VPVIGFIGRL EEQKGSDILV
EAISKFMGLN VQMVILGTGK KKMEAQILEL EEKFPGKAVG VAKFNVPLAH MITAGADFII
VPSRFEPCGL IQLHAMRYGT VPIVASTGGL VDTVKDGYTG FHIGRFNVKC EVVDPDDVIA
TAKAVTRAVA VYGTSAMQEM VKNCMDQDFS WKGPARLWEK VLLSLNVAGS EAGTEGEEIA
PLAKENVATP
