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Entry version 123 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei39Fructose-1,6-bisphosphate1 Publication1 Publication1
Binding sitei40AMP1 Publication1
Binding sitei46AMP1 Publication1
Binding sitei52AMP1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Nucleotidyltransferase, Transferase
Biological processCarbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GLUC1PADENYLTRANS-MONOMER
ECOL316407:JW3393-MONOMER
MetaCyc:GLUC1PADENYLTRANS-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.27 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00164

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:glgC
Ordered Locus Names:b3430, JW3393
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001952942 – 431Glucose-1-phosphate adenylyltransferaseAdd BLAST430

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A6V1

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6V1

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A6V1

PRoteomics IDEntifications database

More...
PRIDEi
P0A6V1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

mRNA stability is at least partially under the control of CsrA; loss of csrA leads to higher transcript levels, possibly mediated by protein binding to the mRNA (PubMed:7751274).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer; dimer of dimers.

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262502, 297 interactors
852251, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-48147N

Protein interaction database and analysis system

More...
IntActi
P0A6V1, 6 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3430

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A6V1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni194 – 195Alpha-D-glucose 1-phosphate binding2 Publications2
Regioni419 – 423Fructose-1,6-bisphosphate binding1 Publication5
Regioni429 – 431Fructose-1,6-bisphosphate binding1 Publication3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107QQ4 Bacteria
COG0448 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000278607

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6V1

KEGG Orthology (KO)

More...
KOi
K00975

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6V1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.550.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00624 GlgC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00483 NTP_transferase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51161 SSF51161, 1 hit
SSF53448 SSF53448, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02091 glgC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00808 ADP_GLC_PYROPHOSPH_1, 1 hit
PS00809 ADP_GLC_PYROPHOSPH_2, 1 hit
PS00810 ADP_GLC_PYROPHOSPH_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3C0A4C4F5B13D9D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A00721 YUEC

NCBI Reference Sequences

More...
RefSeqi
NP_417888.1, NC_000913.3
WP_000253975.1, NZ_STEB01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76455; AAC76455; b3430
BAE77862; BAE77862; BAE77862

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947942

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3393
eco:b3430

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3527

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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_STEB01000004.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP0A6V1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262502, 297 interactors
852251, 1 interactor
DIPiDIP-48147N
IntActiP0A6V1, 6 interactors
STRINGi511145.b3430

Proteomic databases

EPDiP0A6V1
jPOSTiP0A6V1
PaxDbiP0A6V1
PRIDEiP0A6V1

Genome annotation databases

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

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0374

Phylogenomic databases

eggNOGiENOG4107QQ4 Bacteria
COG0448 LUCA
HOGENOMiHOG000278607
InParanoidiP0A6V1
KOiK00975
PhylomeDBiP0A6V1

Enzyme and pathway databases

UniPathwayiUPA00164
BioCyciEcoCyc:GLUC1PADENYLTRANS-MONOMER
ECOL316407:JW3393-MONOMER
MetaCyc:GLUC1PADENYLTRANS-MONOMER
BRENDAi2.7.7.27 2026

Miscellaneous databases

Protein Ontology

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PROi
PR:P0A6V1

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_sf
PfamiView protein in Pfam
PF00483 NTP_transferase, 1 hit
SUPFAMiSSF51161 SSF51161, 1 hit
SSF53448 SSF53448, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLGC_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A6V1
Secondary accession number(s): P00584, Q2M794
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 123 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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