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GLGL1_ORYSJ
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   03-AUG-2022, entry version 142.
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}.
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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   PRIDE; 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
 
 
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