GLGC_KLEP7
ID GLGC_KLEP7 Reviewed; 431 AA.
AC A6TF49;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=KPN78578_37590; ORFNames=KPN_03796;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79183.1; -; Genomic_DNA.
DR RefSeq; WP_002920566.1; NC_009648.1.
DR AlphaFoldDB; A6TF49; -.
DR SMR; A6TF49; -.
DR STRING; 272620.KPN_03796; -.
DR jPOST; A6TF49; -.
DR EnsemblBacteria; ABR79183; ABR79183; KPN_03796.
DR GeneID; 64293149; -.
DR KEGG; kpn:KPN_03796; -.
DR HOGENOM; CLU_029499_14_1_6; -.
DR OMA; QEWDVDE; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000265; 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.
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_1000051570"
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 386
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
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; 48521 MW; CADCBE09F3C1E5B8 CRC64;
MVRLEKNDPL MLARQLPIKS VALILAGGRG TRLKDLTIKR AKPAVHFGGK FRIIDFALSN
CINSGIRRIG VITQYQSHTL VQHIQRGWSF FSEEMNEFVD LLPAQQRVHG ENWYRGTADA
VTQNLDIISR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIEEASAFGV
MAVDENEKII EFVEKPANPP AMPTDPTKSL ASMGIYVFDA AYLYELLEED DRNENSSHDF
GKDIIPKITE AGMAYAHPFP LSCVQSDPNA EPYWRDVGTL EAYWKANLDL ASVTPELDMY
DQNWPIRTHM ESLPPAKFVQ DRSGSHGMTL NSLVSGGCII SGSVVVQSVL FPRVRVNSFC
NIDSAVLLPD VWVGRSCRLR RCVIDRACVI PEGMVIGENA EEDARRFYRS EEGIVLVTRD
MLRKLGHKQE R
