ID   GLGC_ACTSZ              Reviewed;         431 AA.
AC   A6VP17;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; OrderedLocusNames=Asuc_1354;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74714.1; -; Genomic_DNA.
DR   RefSeq; WP_012073091.1; NC_009655.1.
DR   AlphaFoldDB; A6VP17; -.
DR   SMR; A6VP17; -.
DR   STRING; 339671.Asuc_1354; -.
DR   EnsemblBacteria; ABR74714; ABR74714; Asuc_1354.
DR   KEGG; asu:Asuc_1354; -.
DR   eggNOG; COG0448; Bacteria.
DR   HOGENOM; CLU_029499_14_1_6; -.
DR   OMA; YRMDFSQ; -.
DR   OrthoDB; 1557977at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001114; 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..431
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_1000212296"
FT   BINDING         108
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         174
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         189..190
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         207
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ   SEQUENCE   431 AA;  48491 MW;  BCC928221B6FE334 CRC64;
     MSKVITKYDL VGDTLVLILA GGRGSRLHEL TDKRAKPALY FGGNRRIIDF ALSNCINSGL
     NRIGVITQYA AHSLLRHLQT GWSFLPQERG EFVDMLPARQ QIDDNTWYRG TADSVYQNMA
     IIKNHYKPKY ILILAGDHIY KMDYSQMILD HVNSGAKCTV GCIEVPRESA KEFGVMAVNE
     NLKVKAFVEK PSDPPAMIGK PNSSLASMGI YVFNAEYLYE TLERTVNSPQ TSHDFGKDIM
     PMALEDEVLY AHPFDRSCMG RNTEGEIYWR DVGTLDSYWQ SNIDLVSKEP QLDIYDQTWP
     IRGNPVQAYP SKFFYDDPAC KQVDNSLIAG GCVITNASIS YSVLFDNIHV NEGTLIDESV
     ILPQVKVGKN CILKRCIVDR HVQIPDGMQI GVDPEEDSKH FRISSKGIVL VTEKMLQKMK
     GETVKSEDDL D