ID   GLGL2_SOLTU             Reviewed;         519 AA.
AC   P55242;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=AGPS2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=7700228; DOI=10.1007/bf00298960;
RA   la Cognata U., Willmitzer L., Mueller-Roeber B.;
RT   "Molecular cloning and characterization of novel isoforms of potato ADP-
RT   glucose pyrophosphorylase.";
RL   Mol. Gen. Genet. 246:538-548(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. Plastid, amyloplast.
CC       Note=Found in the chloroplast in leaf. Found in the plastid in the
CC       developing endosperm.
CC   -!- TISSUE SPECIFICITY: Leaves and tubers.
CC   -!- DEVELOPMENTAL STAGE: The strongest expression is seen in very small
CC       leaves (less than 1 cm in length) and decreases steadily as leaves
CC       become older. There is approximately 4- to 6-fold stronger expression
CC       in sink leaves relative to source leaves. Only minor variations in
CC       expression are seen during early stages of tuber development, however
CC       expression declines with increase in tuber size.
CC   -!- INDUCTION: By sucrose.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X74982; CAA52917.1; -; mRNA.
DR   PIR; S53991; S53991.
DR   RefSeq; NP_001305598.1; NM_001318669.1.
DR   AlphaFoldDB; P55242; -.
DR   SMR; P55242; -.
DR   STRING; 4113.PGSC0003DMT400041215; -.
DR   PRIDE; P55242; -.
DR   GeneID; 102600909; -.
DR   KEGG; sot:102600909; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   InParanoid; P55242; -.
DR   BRENDA; 2.7.7.27; 5757.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P55242; baseline.
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; 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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..519
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit 2, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011167"
SQ   SEQUENCE   519 AA;  57400 MW;  0BF301793131AF37 CRC64;
     MDALCASMKG TAQLVAICNQ ESAFWGEKIS GRRLINKGFG VRSCKSFTTQ QRGRNVTPAV
     LTRDINKEML PFEESMFEEQ PTADPKAVAS VILGGGVGTR LFPLTSRRAK PAVPIGGCYR
     LIDVPMSNCI NSGIRKIFIL TQFNSFSLNR HLATYNFGNG VGFGDGFVEV LAGTQTPGDG
     RKMWFQAADA VREFIWVFEN QKNKNVEHII ILSGDHLYRM NYMDFVQKHI DTNADITVSC
     VPMDDGRASD FGLMKIDETG AIIQFAEKPK GPALKAMQVD TSILGLSEQE ASNFPYIASM
     GVYVFKTDVL LNLLKSAYPS CNDFGSEIIP SAVKDHNVQA YLFNDYWEDI GTVKSFFDAN
     LALTKQPPKF DFNDPKTPFY TSARFLPPTK VDKSRIVDAI ISHGCFLREC NIQHSIVGVR
     SRLDYGVEFK DTMMMGADYY QTECEIASLL AEGKVPIGVG PNTKIQNCII DKNAKIGKDV
     VILNKEGVEE ADRSAEGFYI RSGITVIMKN ATIKDGTVI