GLGC_NOSS1
ID GLGC_NOSS1 Reviewed; 429 AA.
AC P30521;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}; Synonyms=agp;
GN OrderedLocusNames=all4645;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1325205; DOI=10.1007/bf00029147;
RA Charng Y., Kakefuda G., Iglesias A.A., Buikema W.J., Preiss J.;
RT "Molecular cloning and expression of the gene encoding ADP-glucose
RT pyrophosphorylase from the cyanobacterium Anabaena sp. strain PCC 7120.";
RL Plant Mol. Biol. 20:37-47(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(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 ECO:0000305|PubMed:1325205}.
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: Activated by 3-phosphoglycerate and inhibited by
CC phosphate. {ECO:0000269|PubMed:1325205}.
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; Z11539; CAA77640.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76344.1; -; Genomic_DNA.
DR PIR; AE2386; AE2386.
DR PIR; S24991; S24991.
DR RefSeq; WP_010998776.1; NZ_RSCN01000020.1.
DR AlphaFoldDB; P30521; -.
DR SMR; P30521; -.
DR STRING; 103690.17133782; -.
DR EnsemblBacteria; BAB76344; BAB76344; BAB76344.
DR KEGG; ana:all4645; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; QEWDVDE; -.
DR OrthoDB; 1557977at2; -.
DR BRENDA; 2.7.7.27; 319.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
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:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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..429
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195273"
FT BINDING 162
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 177..178
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 209
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ SEQUENCE 429 AA; 48341 MW; 39FAB8279E5ED377 CRC64;
MKKVLAIILG GGAGTRLYPL TKLRAKPAVP VAGKYRLIDI PVSNCINSEI FKIYVLTQFN
SASLNRHIAR TYNFSGFSEG FVEVLAAQQT PENPNWFQGT ADAVRQYLWM LQEWDVDEFL
ILSGDHLYRM DYRLFIQRHR ETNADITLSV IPIDDRRASD FGLMKIDNSG RVIDFSEKPK
GEALTKMRVD TTVLGLTPEQ AASQPYIASM GIYVFKKDVL IKLLKEALER TDFGKEIIPD
AAKDHNVQAY LFDDYWEDIG TIEAFYNANL ALTQQPMPPF SFYDEEAPIY TRARYLPPTK
LLDCHVTESI IGEGCILKNC RIQHSVLGVR SRIETGCMIE ESLLMGADFY QASVERQCSI
DKGDIPVGIG PDTIIRRAII DKNARIGHDV KIINKDNVQE ADRESQGFYI RSGIVVVLKN
AVITDGTII
