GLGC_SALTY
ID GLGC_SALTY Reviewed; 431 AA.
AC P05415;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
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=STM3536;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040691; DOI=10.1128/jb.169.9.4355-4360.1987;
RA Leung P.S.C., Preiss J.;
RT "Biosynthesis of bacterial glycogen: primary structure of Salmonella
RT typhimurium ADPglucose synthetase as deduced from the nucleotide sequence
RT of the glgC gene.";
RL J. Bacteriol. 169:4355-4360(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; M17363; AAA27132.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22396.1; -; Genomic_DNA.
DR RefSeq; NP_462437.1; NC_003197.2.
DR RefSeq; WP_000253995.1; NC_003197.2.
DR AlphaFoldDB; P05415; -.
DR SMR; P05415; -.
DR STRING; 99287.STM3536; -.
DR PaxDb; P05415; -.
DR EnsemblBacteria; AAL22396; AAL22396; STM3536.
DR GeneID; 1255059; -.
DR KEGG; stm:STM3536; -.
DR PATRIC; fig|99287.12.peg.3738; -.
DR HOGENOM; CLU_029499_14_1_6; -.
DR OMA; QEWDVDE; -.
DR PhylomeDB; P05415; -.
DR BioCyc; SENT99287:STM3536-MON; -.
DR BRENDA; 2.7.7.27; 5542.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001014; 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; Reference proteome; Transferase.
FT CHAIN 1..431
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195327"
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"
FT CONFLICT 37
FT /note="T -> A (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="I -> V (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Missing (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> L (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> R (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> Q (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="P -> R (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> E (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="N -> K (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> F (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> D (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> C (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="V -> GH (in Ref. 1; AAA27132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48462 MW; 942E637798549EE0 CRC64;
MVSLEKNDRV MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN
CLNSGIRRIG VITQYQSHTL VQHIQRGWSL FSEEMNEFVD LLPAQQRMKG ENWYRGTADA
VTQNLDIIRR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIKEATAFGV
MAVDESDKII DFVEKPANPP AMPGDASKSL ASMGIYVFDA DYLYELLAAD DKDDASSHDF
GKDIIPKITR EGMAYAHPFP LSCVQSDPQA EPYWRDVGTL EAYWKANLDL ASVTPELDMY
DQNWPIRTHM ESLPPAKFVQ DRSGSHGMTL NSLVSGGCII SGSVVVQSVL FPRVRINSFC
NIDSAVLLPE VWVGRSCRLR RCVIDRACII PEGMVIGENA EEDARRFYRS EEGIVLVTRE
MLRKLQVKQE R
