GLGC_STRCO
ID GLGC_STRCO Reviewed; 399 AA.
AC P72394; Q9RIU5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 122.
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=SCO0961;
GN ORFNames=SCM11.16c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=9401038; DOI=10.1128/jb.179.24.7784-7789.1997;
RA Martin M.C., Schneider D., Bruton C.J., Chater K.F., Hardisson C.;
RT "A glgC gene essential only for the first of two spatially distinct phases
RT of glycogen synthesis in Streptomyces coelicolor A3(2).";
RL J. Bacteriol. 179:7784-7789(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; X89733; CAA61885.1; -; Genomic_DNA.
DR EMBL; AL939107; CAB61927.1; -; Genomic_DNA.
DR PIR; T42041; T42041.
DR RefSeq; NP_625258.2; NC_003888.3.
DR AlphaFoldDB; P72394; -.
DR SMR; P72394; -.
DR STRING; 100226.SCO0961; -.
DR GeneID; 1096384; -.
DR KEGG; sco:SCO0961; -.
DR PATRIC; fig|100226.15.peg.958; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_11; -.
DR InParanoid; P72394; -.
DR OMA; QEWDVDE; -.
DR PhylomeDB; P72394; -.
DR BRENDA; 2.7.7.27; 5998.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001973; 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..399
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195333"
FT BINDING 158
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 174..175
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 192
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT CONFLICT 20
FT /note="D -> A (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="FG -> L (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..178
FT /note="AD -> PN (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..184
FT /note="AD -> GH (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> P (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> Y (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="Missing (in Ref. 1; CAA61885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42744 MW; 438EDB631483475C CRC64;
MLGIVLAGGE GKRLMPLTAD RAKPAVTFGG TYRLVDFVLS NLVNGDILRI CVLTQYKSHS
LDRHITTTWR MSSLLGNYVT PVPAQQRLGP RWFLGSADAI LQSLNLVHDE QPEYVAVFGA
DHVYRMDPRQ MLAQHIESGA GVTVAGIRVP RAESPSFGVI TPGSDGQTVT GFLEKPADPP
GLADDPGCVF ASMGNYVFTT KALVEALHRD AEDPDSVHDM GGSILPQLTD RGEAALYDFS
ANHVPGETTR DQGYWRDVGT LDAYYDAHMD LIAERPAFNL YNRDWPVYTH STQLSPARFN
AGGIASESII SAGCLIRGQV TRSVLSPGVV VDPGAVVQGS VLHDNVHIGR GAVVRGAVLD
KNVQVPPGAT IGVNPQRDGE LYTVSKGGVI ALGKGQRVP
