ID   GLGL2_MAIZE             Reviewed;         521 AA.
AC   P55234;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 2, 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;
GN   Name=AGP2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 22; TISSUE=Ear of corn;
RX   PubMed=7630966; DOI=10.1104/pp.108.3.1333;
RA   Giroux M., Smith-White B., Gilmore V., Hannah L.C., Preiss J.;
RT   "The large subunit of the embryo isoform of ADP glucose pyrophosphorylase
RT   from maize.";
RL   Plant Physiol. 108:1333-1334(1995).
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: Activated by 3'phosphoglycerate, inhibited by
CC       orthophosphate. Allosteric regulation.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBUNIT: Heterotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Plastid,
CC       amyloplast {ECO:0000250}. Note=Found in the chloroplast in leaf. Found
CC       in the plastid in developing endosperm.
CC   -!- TISSUE SPECIFICITY: Abundant in the embryo and is also present in the
CC       endosperm.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; Z38111; CAA86227.1; -; mRNA.
DR   PIR; S49439; S49439.
DR   AlphaFoldDB; P55234; -.
DR   SMR; P55234; -.
DR   STRING; 4577.GRMZM2G027955_P01; -.
DR   PRIDE; P55234; -.
DR   MaizeGDB; 113181; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P55234; 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   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..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..521
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit 2, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011166"
SQ   SEQUENCE   521 AA;  57989 MW;  9BF611A305257899 CRC64;
     MQFSSVLPLE GKACMSPVRR GSGGYGSERM RINCCSIRRN KALRRMCFSA RGAVSSTQCV
     LTSDAGPDTL VRPNHPFRRN YADPNEVAAV ILGGGTGTQL FPLTSTRATP AVPIGGCYRL
     IDIPMSNCFN SGINKIFVMT QFNSASLNRH IHRTYLGGGI NFTDGSVEVL AATQMPGEAA
     GWFQGTADAV RKFIWVLEDY YKHKAIEHIL ILSGDQLYRM DYMELVQKHV DDNADITLSC
     APVGESRASD YGLVKFDSSG RVIQFSEKPK GAALEEMKVD TSFLNFATCT LPAEYPYIAS
     MGVYVFKRDV LLDLLKSRYA ELHDFGSEIL PKALHEHNVQ AYVFTDYWED IGTIRSFFDA
     NMALCEQPPK FEFYDPKTPF FTSPRYLPPT KSDKCRIKDA IISHGCFLRE CAIEHSIVGV
     PSRLNSGCEL KNTMMMGADL YETEDEISRL LAEGKVPIGV GENTKISNCI IDMNCQGWKE
     RLHNKQRGRS KSPDRPGRRI LIRSGIVVVL KNATIKDGTV I