ID   GLGL1_BETVU             Reviewed;         522 AA.
AC   P55233;
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, 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=AGPS1;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zuchtlinie 5S0026; TISSUE=Tap root;
RX   PubMed=7865789; DOI=10.1007/bf00019190;
RA   Mueller-Roeber B., Nast G., Willmitzer L.;
RT   "Isolation and expression analysis of cDNA clones encoding a small and a
RT   large subunit of ADP-glucose pyrophosphorylase from sugar beet.";
RL   Plant Mol. Biol. 27:191-197(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: Prominently expressed in the leaves. A lower level
CC       expression is seen in the roots.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X78900; CAA55516.1; -; mRNA.
DR   PIR; S51944; S51944.
DR   RefSeq; NP_001289992.1; NM_001303063.1.
DR   AlphaFoldDB; P55233; -.
DR   SMR; P55233; -.
DR   PRIDE; P55233; -.
DR   GeneID; 104889614; -.
DR   KEGG; bvg:104889614; -.
DR   BRENDA; 2.7.7.27; 836.
DR   UniPathway; UPA00152; -.
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; Starch biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..522
FT                   /note="Glucose-1-phosphate adenylyltransferase large
FT                   subunit, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011163"
SQ   SEQUENCE   522 AA;  57717 MW;  16AFAA2318AF2CD5 CRC64;
     MDASAAAINV NAHLTEVGKK RFLGERISQS LKGKDLRALF SRTESKGRNV NKPGVAFSVL
     TSDFNQSVKE SLKYEPALFE SPKADPKNVA AIVLGGGAGT RLFPLTSRRA KPAVPIGGCY
     RLIDVPMSNC INSGIRKIFI LTQFNSFSLN RHLARTYNFG DGVNFGDGFV EVFAATQTPG
     ESGKKWFQGT ADAVRQFFWA FEDSKSKDVE HIVILSGDHL YRMDYMSFWQ KHIDTNADIT
     VSCIPMDDSR ASDYGLMKID HTGRIVHFAE KPKGSDLTAM QVDTTVLGLS DLEAMSNPYI
     ASMGVYVFRT DVLMELLNRK YPSSNDFGSE IIPSAVGESN VQAYLFNDYW EDIGTIKSFF
     DSNLALTQQP PKFEFYDPKT PFYTSARFLP PTKVDRCKIV DSIVSHGCFL QESSIQHSIV
     GVRSRLESGV EFQDTMMMGA DYYQTESEIA SLLAEGKVPV GVGQNTKIKN CIIDKNAKIG
     KDVVIANTDG VEEADRPNEG FYIRSGITII LKNATIQDGL VI