ID   GLGC_GRABC              Reviewed;         417 AA.
AC   Q0BPL4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=GbCGDNIH1_2340;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI63238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000394; ABI63238.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_025319829.1; NC_008343.2.
DR   AlphaFoldDB; Q0BPL4; -.
DR   SMR; Q0BPL4; -.
DR   STRING; 391165.GbCGDNIH1_2340; -.
DR   EnsemblBacteria; ABI63238; ABI63238; GbCGDNIH1_2340.
DR   GeneID; 56916712; -.
DR   KEGG; gbe:GbCGDNIH1_2340; -.
DR   eggNOG; COG0448; Bacteria.
DR   HOGENOM; CLU_029499_14_1_5; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001963; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.550.10; -; 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; 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   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..417
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_0000261873"
FT   BINDING         105
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         170
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         185..186
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         203
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ   SEQUENCE   417 AA;  46154 MW;  C680E405066887AB CRC64;
     MSGTSSIARS TMAYVLAGGR GSRLLELTDT RAKPAVYFGG KSRIIDFALS NAVNSGIRRI
     GVATQYKAHS LIRHMQRGWN FFRPERNEGF DILPASQRVS ETQWYEGTAD AVYQNLDIIA
     GYEPEYMIIL AGDHIYKMDY EIMLHQHVER QADVTVGCIE VPREEATGFG VMQVDDTGRI
     TAFLEKPSDP PGMPGQPDIA LASMGIYVFK TKFLFDVLRR DAADPDSKHD FGGDIIPDLV
     ENGTAIAHRF SDSCVRSSKT AEAYWRDVGT LDSYWQANLD LTNVVPTLDL YDSGWPIWTY
     NEISPPAKFV YDDVGRRGMA VDSLVAGGCI VSGASLSRSL ISTGCRVHSF SQLHGTVVLP
     YADIARSARL RNTVVDRGVR IPEGLVVGED PELDAKRFRR TEKGICLITQ PMIDRLG