GLGL3_ORYSJ
ID GLGL3_ORYSJ Reviewed; 519 AA.
AC Q688T8; O23809; Q0DFN5; Q9XHV4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic/amyloplastic {ECO:0000305};
DE Short=OsAGPL3 {ECO:0000303|PubMed:17406793};
DE Short=OsAPL3 {ECO:0000303|PubMed:15821022};
DE EC=2.7.7.27 {ECO:0000305|PubMed:17406793};
DE AltName: Full=ADP-glucose pyrophosphorylase AGPL3 {ECO:0000305};
DE AltName: Full=ADP-glucose synthase AGPL3 {ECO:0000305};
DE Flags: Precursor;
GN Name=AGPL3 {ECO:0000303|PubMed:17406793};
GN Synonyms=APL3 {ECO:0000303|PubMed:15821022};
GN OrderedLocusNames=Os05g0580000 {ECO:0000312|EMBL:BAF18338.2},
GN LOC_Os05g50380 {ECO:0000305};
GN ORFNames=10A19I.12 {ECO:0000312|EMBL:AAD39597.1},
GN OsJ_19673 {ECO:0000312|EMBL:EEE64817.1},
GN OSJNBa0017N18.13 {ECO:0000312|EMBL:AAU10700.1};
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 [GENOMIC DNA].
RX PubMed=20018713; DOI=10.1073/pnas.0912396106;
RA Tian Z., Qian Q., Liu Q., Yan M., Liu X., Yan C., Liu G., Gao Z., Tang S.,
RA Zeng D., Wang Y., Yu J., Gu M., Li J.;
RT "Allelic diversities in rice starch biosynthesis lead to a diverse array of
RT rice eating and cooking qualities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21760-21765(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endosperm;
RA Satozawa T., Akagi H., Sakamoto M., Baba T., Shimada H., Fujimura T.;
RT "A nucleotide sequence of a large subunit of ADP glucose pyrophosphorylase
RT cDNA from developing seeds of rice.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of the ADP-glucose pyrophosphorylase genes in rice.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [9]
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 [10]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
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 [11]
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. {ECO:0000305|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}.
CC -!- TISSUE SPECIFICITY: Expressed in stems. {ECO:0000269|PubMed:15821022}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 4 to 12 days
CC after flowering (DAF). {ECO:0000269|PubMed:15821022}.
CC -!- INDUCTION: Induced by sucrose, glucose and abscisic acid (ABA).
CC {ECO:0000269|PubMed:15821022}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ150829; ACY56044.1; -; Genomic_DNA.
DR EMBL; GQ150830; ACY56045.1; -; Genomic_DNA.
DR EMBL; GQ150831; ACY56046.1; -; Genomic_DNA.
DR EMBL; GQ150832; ACY56047.1; -; Genomic_DNA.
DR EMBL; GQ150833; ACY56048.1; -; Genomic_DNA.
DR EMBL; GQ150834; ACY56049.1; -; Genomic_DNA.
DR EMBL; D50317; BAA23490.1; -; mRNA.
DR EMBL; EU267957; ACA50479.1; -; mRNA.
DR EMBL; AC007858; AAD39597.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC120988; AAU10700.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18338.2; -; Genomic_DNA.
DR EMBL; AP014961; BAS95514.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64817.1; -; Genomic_DNA.
DR EMBL; AK100910; BAG94825.1; -; mRNA.
DR PIR; T02965; T02965.
DR RefSeq; XP_015640472.1; XM_015784986.1.
DR RefSeq; XP_015640473.1; XM_015784987.1.
DR AlphaFoldDB; Q688T8; -.
DR SMR; Q688T8; -.
DR STRING; 4530.OS05T0580000-01; -.
DR PaxDb; Q688T8; -.
DR PRIDE; Q688T8; -.
DR EnsemblPlants; Os05t0580000-01; Os05t0580000-01; Os05g0580000.
DR GeneID; 4339718; -.
DR Gramene; Os05t0580000-01; Os05t0580000-01; Os05g0580000.
DR KEGG; osa:4339718; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; Q688T8; -.
DR OMA; RKWPLHT; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 4460.
DR PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
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; ATP-binding; Chloroplast; Nucleotide-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Starch biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..519
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 3, chloroplastic/amyloplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441126"
FT CONFLICT 406
FT /note="F -> L (in Ref. 2; BAA23490)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="E -> G (in Ref. 2; BAA23490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 57654 MW; 6BF95E2E3495A3C0 CRC64;
MQFSSVFPLE GKACVSPIRR GGEGSASDRL KIGDSSSIKH DRAVRRMCLG YRGTKNGAQC
VLTSDAGPDT LHVRTSFRRN FADPNEVAAV ILGGGTGTQL FPLTSTRATP AVPIGGCYRL
IDIPMSNCFN SGINKIFIMT QFNSASLNRH IHRTYLGGGI NFTDGSVEVL AATQMPGEAA
GWFQGTADAV RKFIWVLEDY YKHKAIEHIL ILSGDQLYRM DYMELVQKHV DDNADITLSC
APVGESRASD YGLVKFDSSG RVIQFSEKPK GTDLEAMKVD TSFLNFAIDD PTKFPYIASM
GVYVFKRDVL LNLLKSRYAE LHDFGSEILP RALHEHNVQA YVFADYWEDI GTIRSFFDAN
MALCEQPPKF EFYDPKTPFF TSPRYLPPTK SDKCRIKDAI ISHGCFLREC TIEHSIVGVR
SRLNSACELK NTMMMGADLY ETEDEISRLL SEGKVPIGVG ENTKINNCII DMNARVGRNV
VITNSEGVQE SDRPEEGYYI RSGIVVILKN ATIKDGKVI
