ID   GLGC_ALTMD              Reviewed;         431 AA.
AC   B4RS18; F2G9E1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=MADE_1008400;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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; CP001103; AEA97820.1; -; Genomic_DNA.
DR   RefSeq; WP_012518152.1; NC_011138.3.
DR   AlphaFoldDB; B4RS18; -.
DR   SMR; B4RS18; -.
DR   EnsemblBacteria; AEA97820; AEA97820; MADE_1008400.
DR   KEGG; amc:MADE_1008400; -.
DR   HOGENOM; CLU_029499_14_1_6; -.
DR   OMA; QEWDVDE; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001870; 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   Transferase.
FT   CHAIN           1..431
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_1000130464"
FT   BINDING         109
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         175
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         190..191
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         208
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;  48422 MW;  91471F5D6FB1FE23 CRC64;
     MADQSSRYIS NLTRDTYALI LAGGKGSRLH ELTTWRAKPA LYFGGKFRII DFPLSNCVNS
     GIRRIGVVTQ YKSHSLIRHL VRGWGHFKKE LGESVEILPA SQRFSDSWYE GTADAVFQNI
     DIIRDELPKY VMILSGDHIY RMDYGDMLAK HKESGAKMTV SCMSVPLEEA AGAFGVMSVD
     ENYRINGFEE KPANPTPLPN DPTRCLASMG NYVFDTEFLF EQLRVDSENM GSQRDFGKDI
     IPSIIADHPV YAYPFEQSGG DNAYWRDVGT IDSFWEANME MVAPVPQLNL YDRKWPIWTY
     QEQLPPAKFV WEDHDRRGEA INSVVSGGCI ISGSTLRSSI CFSNVRVHSY GLIEDAVILP
     DVEIKRHCKL KRVIIDRGCV IPEGTTIGYD LEQDKARGFR VSEKGVVLVT REMLGQPVGG
     LSQAPNISIT L