ID   GLGS_WHEAT              Reviewed;         473 AA.
AC   P30523;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase small 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 B;
DE   AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE   Flags: Precursor;
GN   Name=AGP-S;
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. Chinese Spring; TISSUE=Grain;
RX   PubMed=8219053; DOI=10.1007/bf00021416;
RA   Ainsworth C.C., Tarvis M.D.R., Clark J.;
RT   "Isolation and analysis of a cDNA clone encoding the small subunit of ADP-
RT   glucose pyrophosphorylase from wheat.";
RL   Plant Mol. Biol. 23:23-33(1993).
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   -!- TISSUE SPECIFICITY: Abundantly expressed in the whole grains, a
CC       slightly less abundant expression is seen in leaves, while a low level
CC       expression is seen in the roots. A greater expression is seen in the
CC       endosperm than in the embryo and pericarp layers.
CC   -!- DEVELOPMENTAL STAGE: Is expressed prior to 10 dpa (days post anthesis),
CC       accumulates to the highest levels between 20 and 35 dpa and levels
CC       decrease after 35 dpa.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X66080; CAA46879.1; -; mRNA.
DR   PIR; S39504; S39504.
DR   AlphaFoldDB; P30523; -.
DR   SMR; P30523; -.
DR   STRING; 4565.Traes_7DS_02539EB3B.1; -.
DR   PRIDE; P30523; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   BRENDA; 2.7.7.27; 6500.
DR   SABIO-RK; P30523; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P30523; 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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..473
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011158"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  52147 MW;  64A4E316CD9260A6 CRC64;
     MDVPLASKTF PSPSPSKREQ CNIDGHKSSS KHADLNPHVD DSVLGIILGG GAGTRLYPLT
     KKRAKPAVPL GANYRLIDIP VSNCLNSNIS KIYVRTQFNS ASLNRHLSRA YGSNIGGYKN
     EGFVEVLAAQ QSPDNPDWFQ GTADAVRQYL WLFEEHNVME YLILAGDHLY RMDYEKFIQA
     HRETDADITV AALPMDEERA TAFGLMKIDE EGRIIEFAEK PKGEQLKAMM VDTTILGLDD
     ARAKEMPYIA SMGIYVISKH VMLQLLREQF PGANDFGSEV IPGATSTGMR VQAYLYDGYW
     EDIGTIEAFY NANLGITKKP IPDFSFYDRS APIYTQPRHL PPSKVLDADV TDSVIGEGCV
     IKNCKIHHSV VGLRSCISEG AIIEDTLLMG ADYYETEADK KLLAEKGGIP IGIGKNSHIK
     RAIIDKNARI GDNVMIINVD NVQEAARETD GYFIKSGIVT VIKDALLPSG TVI