ID   GLGL3_WHEAT             Reviewed;         500 AA.
AC   P12300;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit, chloroplastic/amyloplastic;
DE            EC=2.7.7.27;
DE   AltName: Full=ADP-glucose pyrophosphorylase;
DE   AltName: Full=ADP-glucose synthase;
DE   AltName: Full=AGPase S;
DE   AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE   Flags: Precursor; Fragment;
GN   Name=AGA.7;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Mardler; TISSUE=Endosperm;
RA   Olive M.R., Ellis R.J., Schuch W.W.;
RT   "Isolation and nucloetide sequences of cDNA clones encoding ADP-glucose
RT   pyrophosphorylase polypeptides from wheat leaf and endosperm.";
RL   Plant Mol. Biol. 12:525-538(1989).
CC   -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC       catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC       from Glc-1-P and ATP.
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   -!- ACTIVITY REGULATION: Insensitive to 3'phosphoglycerate and
CC       orthophosphate.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBUNIT: Heterotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC       Note=Found in the chloroplast in leaf. Found in the plastid in the
CC       developing endosperm.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X14350; CAA32533.1; -; mRNA.
DR   PIR; S05077; S05077.
DR   AlphaFoldDB; P12300; -.
DR   SMR; P12300; -.
DR   PRIDE; P12300; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P12300; 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   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast;
KW   Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW   Starch biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         <1..33
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..500
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011170"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   500 AA;  55560 MW;  A266E5D7366E6295 CRC64;
     RASPPSESRA PLRAPQRSAT RQHQARQGPR RMCNGGRGPP YWTAGVTSAP ARQTPLFSGR
     PSGGLSDPNE VAAVILGGGT GTQLFPLTST RATPAVPIGG CYRLIDIPMS NCFNSGINKI
     FVMTQFNSAS LNRHIHRTYL GGGINFTDGS VEVLAATQMP GEAAGWFRGT ADAWRKIIWV
     LEDYYKNKSI EHILILSGDQ LYRMDYMELV QKHVDDNADI TLSCAPVGES RASEYGLVKF
     DSSGRVVQFS EQPKGDDLEA MKVDTSFLNF AIDDPAKYPY IASMGVYVFK RDVLLNLLKS
     RYAELHDFGS EILPRALHDH NVQAYVFTDY WEDIGTIRSF FDANRALCEQ PPKFEFYDPK
     TPFFTSPRYL PPTKSDKCRI KEAIILHGCF LRECKIEHTA FSRLNSGSEL KNAMMMGADS
     YETEDEMSRL MSEGKVPIGV GENTKISNCI IDMNARIGRD VVISNKEGVQ EADRPEEGYY
     IRSGIVVIQK NATIKDGTVV