AC   MF_00624;
DC   Protein; auto
TR   HAMAP; MF_00624; -; 1; level=0
XX
Names: GlgC
XX
ID   GLGC
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase;
DE            EC=2.7.7.27;
DE   AltName: Full=ADP-glucose pyrophosphorylase;
DE            Short=ADPGlc PPase;
DE   AltName: Full=ADP-glucose synthase;
GN   Name=glgC;
XX
case <OC:Mycobacterium>
CC   -!- FUNCTION: Involved in the biosynthesis of ADP-glucose, a building
CC       block, required in the biosynthesis of maltose-1-phosphate (M1P) and in
CC       the elongation reactions to produce linear alpha-1,4-glucans. Catalyzes
CC       the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to
CC       produce pyrophosphate and ADP-Glc.
else
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.
end case
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   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
case <OC:Enterobacteriaceae>
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose-1,6-
CC       bisphosphate (F16BP) and inhibited by AMP.
end case
case not <OC:Mycobacterium>
CC   -!- SUBUNIT: Homotetramer.
end case
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family.
XX
DR   Pfam; PF00483; NTP_transferase; 1; trigger=no
DR   Pfam; PF00132; Hexapep; 0-4; trigger=no
DR   NCBIfam; TIGR02091; GlgC; 1; trigger=no
DR   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1; trigger=no
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1; trigger=no
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1; trigger=no
XX
KW   ATP-binding
KW   Carbohydrate metabolism
KW   Glycogen biosynthesis
KW   Glycogen metabolism
KW   Nucleotide-binding
KW   Nucleotidyltransferase
KW   Transferase
case <OC:Enterobacteriaceae>
KW   Allosteric enzyme
end case
XX
GO   GO:0008878; F:glucose-1-phosphate adenylyltransferase activity
GO   GO:0005978; P:glycogen biosynthetic process
XX
FT   From: GLGC_ECOLI (P0A6V1)
FT   BINDING         194..195
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT   Condition: E-K
case <OC:Enterobacteriaceae>
FT   BINDING         419..423
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT   Condition: R-[ED]-x(2)-R
FT   BINDING         429..431
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT   Condition: Q-E-R
FT   BINDING         39
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT   Condition: K
FT   BINDING         40
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
FT   BINDING         46
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: H
FT   BINDING         52
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
end case
FT   BINDING         114
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT   Condition: Y
case <OC:Enterobacteriaceae>
FT   BINDING         130
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: R
end case
FT   BINDING         179
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT   Condition: G
FT   BINDING         212
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT   Condition: S
case <OC:Enterobacteriaceae>
FT   BINDING         370
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: [ED]
FT   BINDING         386
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT   Condition: [RK]
end case
FT   SITE            74
FT                   /note="Could play a key role in the communication between
FT                   the regulatory and the substrate sites"
FT   Condition: Q
FT   SITE            113
FT                   /note="Could play a key role in the communication between
FT                   the regulatory and the substrate sites"
FT   Condition: [WF]
XX
Size: 376-476;
Related: None;
Template: P0A6V1; P30521; P9WN43;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in ALKEH, PSEA6, VIBCH, VIBPA, VIBVU, VIBVY
Plasmid: None
Comments: GlgC from M.tuberculosis is involved in the biosynthesis of both
 glycogen and capsular alpha-D-glucan.
XX
# Revision 1.30 2023/06/01
//