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Protein

Glucose-1-phosphate adenylyltransferase

Gene

glgC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.1 Publication

Miscellaneous

Displays cooperative behavior and a bibi mechanism with sequential binding of ATP and G1P, followed by ordered release of pyrophosphate and ADP-Glc.1 Publication

Catalytic activityi

ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose.1 Publication

Enzyme regulationi

Allosterically activated by fructose-1,6-bisphosphate (F16BP), hexanediol 1,6-bisphosphate, NADPH and pyridoxal phosphate. Inhibited by AMP and by high concentrations of MgCl2.3 Publications

Kineticsi

Kcat is 111 sec(-1) for adenylyltransferase activity. Kcat is 81 sec(-1) for pyrophosphorylase activity.1 Publication
  1. KM=25 µM for alpha-D-glucose 1-phosphate1 Publication
  2. KM=120 µM for diphosphate1 Publication
  1. Vmax=133 µmol/min/mg enzyme toward alpha-D-glucose 1-phosphate1 Publication
  2. Vmax=97 µmol/min/mg enzyme toward diphosphate1 Publication

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.Curated
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39Fructose-1,6-bisphosphate1 Publication1 Publication1
Binding sitei40AMP1 Publication1
Binding sitei46AMP1 Publication1
Binding sitei52AMP1 Publication1
Sitei74Could play a key role in the communication between the regulatory and the substrate sites1 Publication1
Sitei113Could play a key role in the communication between the regulatory and the substrate sites1 Publication1
Binding sitei114Alpha-D-glucose 1-phosphate1 Publication1
Binding sitei130AMP1 Publication1
Binding sitei179Alpha-D-glucose 1-phosphate; via amide nitrogen1 Publication1
Binding sitei212Alpha-D-glucose 1-phosphate; via carbonyl oxygen1 Publication1
Binding sitei370AMP1 Publication1
Binding sitei386AMP1 Publication1

GO - Molecular functioni

  • AMP binding Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • glucose-1-phosphate adenylyltransferase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

  • glycogen biosynthetic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUC1PADENYLTRANS-MONOMER.
MetaCyc:GLUC1PADENYLTRANS-MONOMER.
BRENDAi2.7.7.27. 2026.
UniPathwayiUPA00164.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-1-phosphate adenylyltransferaseCurated (EC:2.7.7.271 Publication)
Alternative name(s):
ADP-glucose pyrophosphorylase1 Publication
Short name:
ADPGlc PPase1 Publication
ADP-glucose synthase1 Publication
Gene namesi
Name:glgC
Ordered Locus Names:b3430, JW3393
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10379. glgC.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39K → E: The level of activation by pyridoxal phosphate and fructose-1,6-phosphate is only approximately 2-fold compared to activation of 15- to 28-fold respectively, for the wild-type. NADPH is unable to activate the mutant enzyme. 1 Publication1
Mutagenesisi74Q → A: Insensitive to activation by fructose-1,6-bisphosphate, but still binds fructose-1,6-bisphosphate with similar affinity as the wild-type. AMP causes similar inhibition on the wild-type and mutant. 1 Publication1
Mutagenesisi74Q → E: Insensitive to activation by fructose-1,6-bisphosphate. 1 Publication1
Mutagenesisi74Q → N: The enzyme is activated 35-fold by fructose-1,6-bisphosphate. 1 Publication1
Mutagenesisi113W → A: Insensitive to activation by fructose-1,6-bisphosphate, but still binds fructose-1,6-bisphosphate, with similar affinity as the wild-type. AMP causes similar inhibition on the wild-type and mutant. 1 Publication1
Mutagenesisi113W → L: The enzyme is activated only 3-fold by fructose-1,6-bisphosphate. 1 Publication1
Mutagenesisi113W → Y: The enzyme is activated 15-fold by fructose-1,6-bisphosphate. 1 Publication1
Mutagenesisi114Y → F: Shows a decrease of affinity for the substrates and less than 2-fold activation by fructose 1,6-bisphosphate in the ADP-glucose synthesis direction. In contrast, in the pyrophosphorolysis direction, the mutant shoqws about a 30-fold activation by fructose 1,6-bisphosphate. 1 Publication1
Mutagenesisi195K → E, I, H or R: Decrease of the affinity for alpha-D-glucose 1-phosphate, but no loss in adenylyltransferase activity. 1 Publication1
Mutagenesisi195K → Q: 600-fold decrease of the affinity for alpha-D-glucose 1-phosphate compared to the wild-type. In contrast, kinetic constants for ATP, magnesium and fructose-1,6-bisphosphate are similar in mutant and wild-type cases. The catalytic efficiency is 2-fold lower in the mutant. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001952942 – 431Glucose-1-phosphate adenylyltransferaseAdd BLAST430

Proteomic databases

PaxDbiP0A6V1.
PRIDEiP0A6V1.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262502. 259 interactors.
DIPiDIP-48147N.
IntActiP0A6V1. 6 interactors.
STRINGi316385.ECDH10B_3604.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 18Combined sources7
Beta strandi20 – 25Combined sources6
Helixi34 – 37Combined sources4
Beta strandi38 – 40Combined sources3
Helixi42 – 44Combined sources3
Turni48 – 50Combined sources3
Helixi54 – 63Combined sources10
Beta strandi68 – 75Combined sources8
Helixi78 – 87Combined sources10
Helixi93 – 95Combined sources3
Beta strandi98 – 103Combined sources6
Beta strandi108 – 110Combined sources3
Helixi117 – 123Combined sources7
Helixi125 – 130Combined sources6
Beta strandi134 – 140Combined sources7
Helixi149 – 158Combined sources10
Beta strandi162 – 171Combined sources10
Helixi172 – 177Combined sources6
Beta strandi178 – 183Combined sources6
Beta strandi187 – 195Combined sources9
Beta strandi208 – 219Combined sources12
Helixi220 – 232Combined sources13
Beta strandi233 – 235Combined sources3
Turni240 – 243Combined sources4
Helixi244 – 250Combined sources7
Beta strandi254 – 258Combined sources5
Helixi259 – 261Combined sources3
Helixi280 – 289Combined sources10
Beta strandi292 – 294Combined sources3
Beta strandi316 – 319Combined sources4
Beta strandi327 – 334Combined sources8
Beta strandi339 – 342Combined sources4
Beta strandi344 – 347Combined sources4
Beta strandi361 – 367Combined sources7
Beta strandi378 – 384Combined sources7
Beta strandi395 – 398Combined sources4
Helixi400 – 406Combined sources7
Beta strandi407 – 409Combined sources3
Beta strandi415 – 417Combined sources3
Helixi419 – 424Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L6SX-ray3.04A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-431[»]
5L6VX-ray2.67A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-431[»]
5MNIX-ray3.09A/B/C/D/E/F/G/H1-431[»]
ProteinModelPortaliP0A6V1.
SMRiP0A6V1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 195Alpha-D-glucose 1-phosphate binding2 Publications2
Regioni419 – 423Fructose-1,6-bisphosphate binding1 Publication5
Regioni429 – 431Fructose-1,6-bisphosphate binding1 Publication3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QQ4. Bacteria.
COG0448. LUCA.
HOGENOMiHOG000278607.
InParanoidiP0A6V1.
KOiK00975.
PhylomeDBiP0A6V1.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00624. GlgC. 1 hit.
InterProiView protein in InterPro
IPR011831. ADP-Glc_PPase.
IPR005836. ADP_Glu_pyroP_CS.
IPR023049. GlgC_bac.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
PfamiView protein in Pfam
PF00483. NTP_transferase. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 2 hits.
TIGRFAMsiTIGR02091. glgC. 1 hit.
PROSITEiView protein in PROSITE
PS00808. ADP_GLC_PYROPHOSPH_1. 1 hit.
PS00809. ADP_GLC_PYROPHOSPH_2. 1 hit.
PS00810. ADP_GLC_PYROPHOSPH_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6V1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK
60 70 80 90 100
FRIIDFALSN CINSGIRRMG VITQYQSHTL VQHIQRGWSF FNEEMNEFVD
110 120 130 140 150
LLPAQQRMKG ENWYRGTADA VTQNLDIIRR YKAEYVVILA GDHIYKQDYS
160 170 180 190 200
RMLIDHVEKG ARCTVACMPV PIEEASAFGV MAVDENDKII EFVEKPANPP
210 220 230 240 250
SMPNDPSKSL ASMGIYVFDA DYLYELLEED DRDENSSHDF GKDLIPKITE
260 270 280 290 300
AGLAYAHPFP LSCVQSDPDA EPYWRDVGTL EAYWKANLDL ASVVPELDMY
310 320 330 340 350
DRNWPIRTYN ESLPPAKFVQ DRSGSHGMTL NSLVSGGCVI SGSVVVQSVL
360 370 380 390 400
FSRVRVNSFC NIDSAVLLPE VWVGRSCRLR RCVIDRACVI PEGMVIGENA
410 420 430
EEDARRFYRS EEGIVLVTRE MLRKLGHKQE R
Length:431
Mass (Da):48,698
Last modified:January 23, 2007 - v2
Checksum:i3C0A4C4F5B13D9D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti161A → V in CAA23544 (PubMed:1320612).Curated1
Sequence conflicti161A → V in AAA98736 (PubMed:1320612).Curated1
Sequence conflicti161A → V in AAA23873 (PubMed:1320612).Curated1
Sequence conflicti166A → V in CAA23544 (PubMed:1320612).Curated1
Sequence conflicti166A → V in AAA98736 (PubMed:1320612).Curated1
Sequence conflicti166A → V in AAA23873 (PubMed:1320612).Curated1
Sequence conflicti189I → T in CAA23544 (PubMed:1320612).Curated1
Sequence conflicti189I → T in AAA98736 (PubMed:1320612).Curated1
Sequence conflicti189I → T in AAA23873 (PubMed:1320612).Curated1
Sequence conflicti296E → K in CAA23544 (PubMed:1320612).Curated1
Sequence conflicti296E → K in AAA98736 (PubMed:1320612).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti44A → T in SG14 mutant; lower apparent affinities for substrates, fructose-1,6-bisphosphate and AMP. 1 Publication1
Natural varianti67R → C in CL1136 mutant; less dependent on the allosteric activator, fructose-1,6-bisphosphate, for activity and less sensitive to inhibition by AMP. 1 Publication1
Natural varianti295P → S in SG5 mutant. 1 Publication1
Natural varianti336G → D in 618 mutant; causes lowered affinity for AMP. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00281 Genomic DNA. Translation: CAA23544.1.
J01616 Genomic DNA. Translation: AAA98736.1.
M97226 Genomic DNA. Translation: AAA23873.1.
S58224 Genomic DNA. Translation: AAB26162.1.
U18997 Genomic DNA. Translation: AAA58228.1.
U00096 Genomic DNA. Translation: AAC76455.1.
AP009048 Genomic DNA. Translation: BAE77862.1.
PIRiA00721. YUEC.
RefSeqiNP_417888.1. NC_000913.3.
WP_000253975.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76455; AAC76455; b3430.
BAE77862; BAE77862; BAE77862.
GeneIDi947942.
KEGGiecj:JW3393.
eco:b3430.
PATRICifig|511145.12.peg.3527.

Similar proteinsi

Entry informationi

Entry nameiGLGC_ECOLI
AccessioniPrimary (citable) accession number: P0A6V1
Secondary accession number(s): P00584, Q2M794
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 107 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families