ID A0A0C7P0T0_DEFTU Unreviewed; 419 AA.
AC A0A0C7P0T0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00624};
DE EC=2.7.7.27 {ECO:0000256|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00624};
DE Short=ADPGlc PPase {ECO:0000256|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose synthase {ECO:0000256|HAMAP-Rule:MF_00624};
GN Name=glgC {ECO:0000256|HAMAP-Rule:MF_00624,
GN ECO:0000313|EMBL:CEP77629.1};
GN ORFNames=DTL3_0298 {ECO:0000313|EMBL:CEP77629.1};
OS Defluviitoga tunisiensis.
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Defluviitoga.
OX NCBI_TaxID=1006576 {ECO:0000313|EMBL:CEP77629.1, ECO:0000313|Proteomes:UP000032809};
RN [1] {ECO:0000313|Proteomes:UP000032809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L3 {ECO:0000313|Proteomes:UP000032809};
RA Wibberg D.;
RL Submitted (NOV-2014) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00624};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00624, ECO:0000256|RuleBase:RU003742}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00624}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443,
CC ECO:0000256|HAMAP-Rule:MF_00624}.
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DR EMBL; LN824141; CEP77629.1; -; Genomic_DNA.
DR RefSeq; WP_045087222.1; NZ_LN824141.1.
DR AlphaFoldDB; A0A0C7P0T0; -.
DR STRING; 1006576.DTL3_0298; -.
DR KEGG; dtn:DTL3_0298; -.
DR PATRIC; fig|1006576.9.peg.295; -.
DR HOGENOM; CLU_029499_14_1_0; -.
DR OrthoDB; 9801810at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000032809; Chromosome I.
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 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 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 NCBIfam; TIGR02091; glgC; 1.
DR PANTHER; PTHR43523:SF2; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00624}; Reference proteome {ECO:0000313|Proteomes:UP000032809};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00624}.
FT DOMAIN 5..256
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT BINDING 97
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 162
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 177..178
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 188
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT SITE 57
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT SITE 96
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
SQ SEQUENCE 419 AA; 46539 MW; 7A02646991CB554A CRC64;
MKVIGIILAG GQGTRLGVLT NTLAKPAVPF GGKYRMIDFT LSNCVNSGIN TVGVATQYMP
HRLVEHLGIG KPWDLDIKGG GLHVLPPYLS RSGTSWYRGT ADAIYQNLEF LDRYKPDFVV
VLSGDHIYKM DYNNMIDYHI EKNADCTIAC MEVPVSEAQR FGIMVTDPFN KIVEFQEKPK
NPKGTLASLG IYVFTWSFLK DSLIEDSKDP NSEHDFGKNI IPKSLAKKSK LYAFGFEGYW
RDVGTIQSYL DSNLELLAPL PLLDLHDESW KVYTQSEELP PAFIANNSEV IKSITSEGSE
IYGTVENSVL FQGVTVAEGA VVKNSVLMNH VFVDKNSYIE QSIIAEKAYI GKSVKIGVGK
FAESKIDKKI YDSEISVIGF HSKITDGIEI GKNCVIDNYV DLSEYNIKQI KSGEGIIKQ
//
