ID   GLGL2_HORVU             Reviewed;         181 AA.
AC   P55239;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 2;
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   AltName: Full=BLPL;
DE   Flags: Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bomi; TISSUE=Leaf;
RX   PubMed=1320425; DOI=10.1007/bf00023385;
RA   Villand P., Aalen R., Olsen O.-A., Luethi E., Loenneborg A.,
RA   Kleczkowski L.A.;
RT   "PCR amplification and sequences of cDNA clones for the small and large
RT   subunits of ADP-glucose pyrophosphorylase from barley tissues.";
RL   Plant Mol. Biol. 19:381-389(1992).
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: Highly active without 3'phosphoglycerate, and is
CC       only slightly affected by the activator 3'phosphoglycerate and
CC       inhibitor 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   -!- TISSUE SPECIFICITY: Leaves.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X62243; CAB37842.1; -; mRNA.
DR   PIR; S22526; S22526.
DR   AlphaFoldDB; P55239; -.
DR   SMR; P55239; -.
DR   SABIO-RK; P55239; -.
DR   UniPathway; UPA00152; -.
DR   ExpressionAtlas; P55239; 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   PANTHER; PTHR43523; PTHR43523; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 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; Starch biosynthesis;
KW   Transferase.
FT   CHAIN           <1..>181
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit 2"
FT                   /id="PRO_0000195356"
FT   NON_TER         1
FT   NON_TER         181
SQ   SEQUENCE   181 AA;  20329 MW;  02FEB6152CB6DA8B CRC64;
     KYPYIAGMGV YIFKKEILLN LLRWRFPTAN DFGSEIIPAA AREINVKAYL FNDYWEDIGT
     IKSFFEANLA LAEQPSKFSF YDASKPMYTS RRNLPPSMIS GSKITDSIIS HGCFLDKCRV
     EHSVVGIRSR IGSNVHLKDT VMLGADFYET DAERGDQLAE GKVPIGIGEN TSIQNCIIDM
     N