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GLGC_SALA4
ID   GLGC_SALA4              Reviewed;         431 AA.
AC   B5F8Q2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=SeAg_B3737;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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   -!- ACTIVITY REGULATION: Allosterically activated by fructose-1,6-
CC       bisphosphate (F16BP) and inhibited by AMP. {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; CP001138; ACH51157.1; -; Genomic_DNA.
DR   RefSeq; WP_000253994.1; NC_011149.1.
DR   AlphaFoldDB; B5F8Q2; -.
DR   SMR; B5F8Q2; -.
DR   EnsemblBacteria; ACH51157; ACH51157; SeAg_B3737.
DR   KEGG; sea:SeAg_B3737; -.
DR   HOGENOM; CLU_029499_14_1_6; -.
DR   OMA; QEWDVDE; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008819; 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   Allosteric enzyme; ATP-binding; Carbohydrate metabolism;
KW   Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..431
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_1000130497"
FT   BINDING         39
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         40
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         46
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         52
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         114
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         130
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         179
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         194..195
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         212
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         370
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         386
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         419..423
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         429..431
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   SITE            74
FT                   /note="Could play a key role in the communication between
FT                   the regulatory and the substrate sites"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   SITE            113
FT                   /note="Could play a key role in the communication between
FT                   the regulatory and the substrate sites"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ   SEQUENCE   431 AA;  48446 MW;  12ECFEFE40C913AB CRC64;
     MVSLEKNDRV MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN
     CLNSGIRRIG VITQYQSHTL VQHIQRGWSL FSEEMNEFVD LLPAQQRMKG ENWYRGTADA
     VTQNLDIIRR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIKEATAFGV
     MAVDESDKII DFVEKPANPP AMPGDASKAL ASMGIYVFDA DYLYELLAAD DKDDASSHDF
     GKDIIPKITR EGMAYAHPFP LSCVQSDPQA EPYWRDVGTL EAYWKANLDL ASVTPELDMY
     DQNWPIRTHM ESLPPAKFVQ DRSGSHGMTL NSLVSGGCII SGSVVVQSVL FPRVRINSFC
     NIDSAVLLPE VWVGRSCRLR RCVIDRACII PEGMVIGENA EEDARRFYRS EEGIVLVTRE
     MLRKLQVKQE R
 
 
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