ID GLGL1_ORYSJ Reviewed; 511 AA. AC Q6AVT2; DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 25-MAY-2022, entry version 141. DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic {ECO:0000305}; DE Short=OsAGPL1 {ECO:0000303|PubMed:17406793}; DE Short=OsAPL1 {ECO:0000303|PubMed:15821022}; DE EC=2.7.7.27 {ECO:0000305|PubMed:17406793}; DE AltName: Full=ADP-glucose pyrophosphorylase AGPL1 {ECO:0000305}; DE AltName: Full=ADP-glucose synthase AGPL1 {ECO:0000305}; DE Flags: Precursor; GN Name=AGPL1 {ECO:0000303|PubMed:17406793}; GN Synonyms=APL1 {ECO:0000303|PubMed:15821022}; GN OrderedLocusNames=Os03g0735000 {ECO:0000312|EMBL:BAF13098.1}, GN LOC_Os03g52460 {ECO:0000312|EMBL:ABF98731.1}; GN ORFNames=OSJNBa0027J18.8 {ECO:0000312|EMBL:AAT78793.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Ilpoombyeo; RA Yoon U.-H., Hahn J.-H.; RT "Structural and expression analysis of immature seed genes in Oryza sativa RT L."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [7] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=15821022; DOI=10.1093/pcp/pci101; RA Akihiro T., Mizuno K., Fujimura T.; RT "Gene expression of ADP-glucose pyrophosphorylase and starch contents in RT rice cultured cells are cooperatively regulated by sucrose and ABA."; RL Plant Cell Physiol. 46:937-946(2005). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR RP LOCATION. RX PubMed=17406793; DOI=10.1007/s11103-007-9153-z; RA Lee S.K., Hwang S.K., Han M., Eom J.S., Kang H.G., Han Y., Choi S.B., RA Cho M.H., Bhoo S.H., An G., Hahn T.R., Okita T.W., Jeon J.S.; RT "Identification of the ADP-glucose pyrophosphorylase isoforms essential for RT starch synthesis in the leaf and seed endosperm of rice (Oryza sativa RT L.)."; RL Plant Mol. Biol. 65:531-546(2007). CC -!- FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis of CC ADP-glucose, a molecule that serves as an activated glycosyl donor for CC alpha-1,4-glucan synthesis. Essential for starch synthesis in leaf CC chloroplasts and endosperm amyloplasts. {ECO:0000269|PubMed:17406793}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498, CC ChEBI:CHEBI:58601; EC=2.7.7.27; CC Evidence={ECO:0000305|PubMed:17406793}; CC -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by CC orthophosphate. Allosteric regulation. {ECO:0000305|PubMed:17406793}. CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}. CC -!- SUBUNIT: Heterotetramer composed of two small and two large subunits. CC {ECO:0000305|PubMed:17406793}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:17406793}. Plastid, amyloplast CC {ECO:0000269|PubMed:17406793}. CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems. CC {ECO:0000269|PubMed:15821022}. CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 10 to 12 days CC after flowering (DAF). {ECO:0000269|PubMed:15821022}. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KT199366; ALC78406.1; -; mRNA. DR EMBL; AC096689; AAT78793.1; -; Genomic_DNA. DR EMBL; DP000009; ABF98731.1; -; Genomic_DNA. DR EMBL; AP008209; BAF13098.1; -; Genomic_DNA. DR EMBL; AP014959; BAS86250.1; -; Genomic_DNA. DR EMBL; AK069296; BAG91362.1; -; mRNA. DR RefSeq; XP_015632018.1; XM_015776532.1. DR AlphaFoldDB; Q6AVT2; -. DR SMR; Q6AVT2; -. DR STRING; 4530.OS03T0735000-01; -. DR PaxDb; Q6AVT2; -. DR EnsemblPlants; Os03t0735000-01; Os03t0735000-01; Os03g0735000. DR GeneID; 4334020; -. DR Gramene; Os03t0735000-01; Os03t0735000-01; Os03g0735000. DR KEGG; osa:4334020; -. DR eggNOG; KOG1322; Eukaryota. DR HOGENOM; CLU_029499_14_4_1; -. DR InParanoid; Q6AVT2; -. DR OMA; YRMDFSQ; -. DR OrthoDB; 806744at2759; -. DR BRENDA; 2.7.7.27; 4460. DR PlantReactome; R-OSA-1119477; Starch biosynthesis. DR UniPathway; UPA00152; -. DR Proteomes; UP000000763; Chromosome 3. DR Proteomes; UP000059680; Chromosome 3. DR ExpressionAtlas; Q6AVT2; baseline and differential. DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro. DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR011831; ADP-Glc_PPase. DR InterPro; IPR005836; ADP_Glu_pyroP_CS. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR PANTHER; PTHR43523; PTHR43523; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR02091; glgC; 1. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1. PE 1: Evidence at protein level; KW Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast; KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome; KW Starch biosynthesis; Transferase; Transit peptide. FT TRANSIT 1..58 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 59..511 FT /note="Glucose-1-phosphate adenylyltransferase large FT subunit 1, chloroplastic/amyloplastic" FT /evidence="ECO:0000255" FT /id="PRO_0000441124" SQ SEQUENCE 511 AA; 55427 MW; 2838EF4380752163 CRC64; MAAMDLRVAA PASVAAAARC GTSLARPWPA RAVGGGGGGG GRGRRLSVRT SVATTEAAAA AVGASEDAAL EARDSKTVVA VILGGGAGTR LFPLTKRRAK PAVPIGGAYR LIDVPMSNCI NSGINKVYIL TQFNSASLNR HLSRAYNFSN GVAFGDGFVE VLAATQTPGS EGKRWFQGTA DAVRQFDWLF DDAKAKDIDD VLILSGDHLY RMDYMDFVQS HRQRGADISI CCLPIDDSRA SDFGLMKIDD TGRVIAFSEK PKGDDLKAMQ VDTTVLGLPQ DEAKEKPYIA SMGVYIFKKE ILLNLLRWRF PTANDFGSEI IPASAKEINV KAYLFNDYWE DIGTIKSFFE ANLSLAEQPP RFSFYDANKP MYTSRRNLPP SMINNSKITD SIISHGCFLD SCRIEHSVVG IRSRIGSNVH LKDTVMLGAD FYETDLERGE LLAEGKVPIG IGENTKIQNC IIDKNARIGK NVTISNSEGV QEADRTSEGF YIRSGITIVL KNSIIADGLV I //