ID   GLGC_SYNY3              Reviewed;         439 AA.
AC   P52415; P74703;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   04-NOV-2026, entry version 150.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00624};
DE            EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00624};
DE            Short=ADPGlc PPase {ECO:0000255|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624};
GN   Name=glgC {ECO:0000255|HAMAP-Rule:MF_00624}; Synonyms=agp;
GN   OrderedLocusNames=slr1176;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-439.
RA   Kakefuda G., Charng Y.Y., Iglesias A.A., McIntosh L., Preiss J.;
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block
CC       required for the elongation reactions to produce glycogen. Catalyzes
CC       the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to
CC       produce pyrophosphate and ADP-Glc. {ECO:0000255|HAMAP-Rule:MF_00624}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00624};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00624}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00624}.
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DR   EMBL; BA000022; BAA18822.1; -; Genomic_DNA.
DR   EMBL; M83556; AAA27275.1; -; Genomic_DNA.
DR   PIR; S76910; S76910.
DR   AlphaFoldDB; P52415; -.
DR   SMR; P52415; -.
DR   FunCoup; P52415; 157.
DR   IntAct; P52415; 2.
DR   STRING; 1148.gene:10500594; -.
DR   PaxDb; 1148-gene:10500594; -.
DR   EnsemblBacteria; BAA18822; BAA18822; BAA18822.
DR   KEGG; syn:slr1176; -.
DR   eggNOG; COG0448; Bacteria.
DR   InParanoid; P52415; -.
DR   OMA; AADWVYA; -.
DR   PhylomeDB; P52415; -.
DR   BioCyc; MetaCyc:MONOMER-20262; -.
DR   BRENDA; 2.7.7.27; 382.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-ARBA.
DR   GO; GO:0010170; C:glucose-1-phosphate adenylyltransferase complex; IBA:GO_Central.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProtKB-ARBA.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019252; P:starch biosynthetic process; IBA:GO_Central.
DR   CDD; cd02508; ADP_Glucose_PP; 1.
DR   CDD; cd04651; LbH_G1P_AT_C; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   HAMAP; MF_00624; GlgC; 1.
DR   InterPro; IPR011831; ADP-Glc_PPase.
DR   InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR   InterPro; IPR023049; GlgC_bac.
DR   InterPro; IPR064045; LbH_GLGC.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR02091; glgC; 1.
DR   NCBIfam; NF002772; PRK02862.1; 1.
DR   PANTHER; PTHR43523:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF25247; LbH_GLGC; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..439
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_0000195338"
FT   BINDING         172
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         187..188
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         219
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   CONFLICT        196
FT                   /note="A -> G (in Ref. 2; AAA27275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  49366 MW;  018BED2B72F9EB93 CRC64;
     MCCWQSRGLL VKRVLAIILG GGAGTRLYPL TKLRAKPAVP LAGKYRLIDI PVSNCINSEI
     VKIYVLTQFN SASLNRHISR AYNFSGFQEG FVEVLAAQQT KDNPDWFQGT ADAVRQYLWL
     FREWDVDEYL ILSGDHLYRM DYAQFVKRHR ETNADITLSV VPVDDRKAPE LGLMKIDAQG
     RITDFSEKPQ GEALRAMQVD TSVLGLSAEK AKLNPYIASM GIYVFKKEVL HNLLEKYEGA
     TDFGKEIIPD SASDHNLQAY LFDDYWEDIG TIEAFYEANL ALTKQPSPDF SFYNEKAPIY
     TRGRYLPPTK MLNSTVTESM IGEGCMIKQC RIHHSVLGIR SRIESDCTIE DTLVMGNDFY
     ESSSERDTLK ARGEIAAGIG SGTTIRRAII DKNARIGKNV MIVNKENVQE ANREELGFYI
     RNGIVVVIKN VTIADGTVI
//