GLGC_RHIRD
ID GLGC_RHIRD Reviewed; 420 AA.
AC P39669;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A348;
RX PubMed=7959036; DOI=10.1016/0378-1119(94)90869-9;
RA Uttaro A.D., Ugalde R.A.;
RT "A chromosomal cluster of genes encoding ADP-glucose synthetase, glycogen
RT synthase and phosphoglucomutase in Agrobacterium tumefaciens.";
RL Gene 150:117-122(1994).
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; AF033856; AAD03473.1; -; Genomic_DNA.
DR PDB; 3BRK; X-ray; 2.10 A; X=1-420.
DR PDB; 5W5R; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/U=6-420.
DR PDB; 5W5T; X-ray; 1.76 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/Z=6-420.
DR PDB; 5W6J; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/U=1-420.
DR PDB; 6VR0; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=6-418.
DR PDBsum; 3BRK; -.
DR PDBsum; 5W5R; -.
DR PDBsum; 5W5T; -.
DR PDBsum; 5W6J; -.
DR PDBsum; 6VR0; -.
DR AlphaFoldDB; P39669; -.
DR SMR; P39669; -.
DR STRING; 1082932.ATCR1_20068; -.
DR eggNOG; COG0448; Bacteria.
DR BRENDA; 2.7.7.27; 200.
DR UniPathway; UPA00164; -.
DR EvolutionaryTrace; P39669; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..420
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195272"
FT BINDING 107
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
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 205
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5W6J"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5W5R"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:5W5R"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:5W5R"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6VR0"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5W5R"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:5W5R"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:5W5R"
SQ SEQUENCE 420 AA; 47029 MW; F93F5E4E5996E698 CRC64;
MSEKRVQPLA RDAMAYVLAG GRGSRLKELT DRRAKPAVYF GGKARIIDFA LSNALNSGIR
RIGVATQYKA HSLIRHLQRG WDFFRPERNE SFDILPASQR VSETQWYEGT ADAVYQNIDI
IEPYAPEYMV ILAGDHIYKM DYEYMLQQHV DSGADVTIGC LEVPRMEATG FGVMHVNEKD
EIIDFIEKPA DPPGIPGNEG FALASMGIYV FHTKFLMEAV RRDAADPTSS RDFGKDIIPY
IVEHGKAVAH RFADSCVRSD FEHEPYWRDV GTIDAYWQAN IDLTDVVPDL DIYDKSWPIW
TYAEITPPAK FVHDDEDRRG SAVSSVVSGD CIISGAALNR SLLFTGVRAN SYSRLENAVV
LPSVKIGRHA QLSNVVIDHG VVIPEGLIVG EDPELDAKRF RRTESGICLI TQSMIDKLDL
