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UniProtKB - P06999 (PFKB_ECOLI)

Entry version 179 (25 May 2022)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

ATP-dependent 6-phosphofructokinase isozyme 2

Gene

pfkB

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

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

1 Publication

Miscellaneous

Only 10% of the activity present in the wild-type strain is phosphofructokinase-2.
This enzyme is not to be confused with 6-phosphofructo-2-kinase which is also called phosphofructokinase 2.
E.coli has two 6-phosphofructokinases enzymes.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 inhibited by ATP. Allosteric ATP-binding requires the presence of the substrate ATP. Inhibited by monovalent cations with ionic radii larger than Na+ (e.g. K+, Cs+). The monovalent cations increase the affinity of the allosteric site for ATP. PFK-2 is sensitive to inhibition by fructose 1,6-diphosphate.2 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

  1. KM=8 µM for ATP1 Publication
  2. KM=6 µM for fructose 6-phosphate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose. This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei27ATP 1; substrate ATP; shared with dimeric partnerCombined sources4 Publications1
Binding sitei27ATP 2; allosteric inhibitor ATP; shared with dimeric partnerCombined sources1 Publication1
Binding sitei139Substrate1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi190Magnesium; catalyticCurated1
Binding sitei248ATP 1; substrate ATPCombined sources4 Publications1
Metal bindingi250Potassium; via carbonyl oxygen1 Publication1
Metal bindingi252Potassium; via carbonyl oxygen1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei256By similarity1
Binding sitei256Substrate1
Binding sitei280ATP 1; via carbonyl oxygen; substrate ATPCombined sources4 Publications1
Binding sitei284ATP 1; substrate ATPCombined sources4 Publications1
Metal bindingi286Potassium; via carbonyl oxygen1 Publication1
Metal bindingi289Potassium; via carbonyl oxygen1 Publication1
Metal bindingi291Potassium; via carbonyl oxygen1 Publication1
Metal bindingi293Potassium; via carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi185 – 187ATP 1; substrate ATPCombined sources4 Publications3
Nucleotide bindingi224 – 229ATP 1; substrate ATPCombined sources4 Publications6

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • glycolytic process Source: EcoCyc
Complete GO annotation on QuickGO ...

<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 functionKinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:6PFK-2-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.1.11, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P06999

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

More...UniPathwayi		UPA00109;UER00182

<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%5Fand%5Ftaxonomy%5Fsection">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:
ATP-dependent 6-phosphofructokinase isozyme 2 (EC:2.7.1.11)
Short name:
ATP-PFK 2
Short name:
Phosphofructokinase 2
Alternative name(s):
6-phosphofructokinase isozyme II
Phosphohexokinase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:pfkB
Ordered Locus Names:b1723, JW5280
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi190E → Q: Causes a 50-fold decrease in the kcat value and a 15-fold increment in the apparent KM for ATP. 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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000800831 – 309ATP-dependent 6-phosphofructokinase isozyme 2Add BLAST309

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06999

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

More...PaxDbi		P06999

PRoteomics IDEntifications database

More...PRIDEi		P06999

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P06999

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P06999
With#Exp.IntAct
itself2EBI-6966085,EBI-6966085

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263076, 25 interactors

Database of interacting proteins

More...DIPi		DIP-10465N

Molecular INTeraction database

More...MINTi		P06999

STRING: functional protein association networks

More...STRINGi		511145.b1723

<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

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P06999

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

More...SMRi		P06999

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06999

<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>Regioni12 – 14Substrate binding3
Regioni27 – 29Substrate binding3
Regioni39 – 43Substrate binding5
Regioni90 – 92Substrate binding3
Regioni187 – 189ATP 2 binding; allosteric inhibitor ATPCombined sources1 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

Belongs to the carbohydrate kinase PfkB family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1105, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_050013_0_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06999

Identification of Orthologs from Complete Genome Data

More...OMAi		QLNEPGP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06999

Family and domain databases

Conserved Domains Database

More...CDDi		cd01164, FruK_PfkB_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.1190.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002173, Carboh/pur_kinase_PfkB_CS
IPR011611, PfkB_dom
IPR029056, Ribokinase-like
IPR017583, Tagatose/fructose_Pkinase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00294, PfkB, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000535, 1PFK/6PFK/LacC, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53613, SSF53613, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03168, 1-PFK, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00583, PFKB_KINASES_1, 1 hit
PS00584, PFKB_KINASES_2, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P06999-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVRIYTLTLA PSLDSATITP QIYPEGKLRC TAPVFEPGGG GINVARAIAH 
        60         70         80         90        100
LGGSATAIFP AGGATGEHLV SLLADENVPV ATVEAKDWTR QNLHVHVEAS 
       110        120        130        140        150
GEQYRFVMPG AALNEDEFRQ LEEQVLEIES GAILVISGSL PPGVKLEKLT 
       160        170        180        190        200
QLISAAQKQG IRCIVDSSGE ALSAALAIGN IELVKPNQKE LSALVNRELT 
       210        220        230        240        250
QPDDVRKAAQ EIVNSGKAKR VVVSLGPQGA LGVDSENCIQ VVPPPVKSQS 
       260        270        280        290        300
TVGAGDSMVG AMTLKLAENA SLEEMVRFGV AAGSAATLNQ GTRLCSHDDT 

QKIYAYLSR
Length:309
Mass (Da):32,456
Last modified:November 1, 1997 - 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:iA93BEBE0D5801309
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 conflicti26 – 38GKLRC…VFEPG → ENCAVPHRCSNP in AAA24321 (PubMed:6235149).CuratedAdd BLAST13
Sequence conflicti26 – 38GKLRC…VFEPG → ENCAVPHRCSNP in AAA24320 (PubMed:6310120).CuratedAdd BLAST13
Sequence conflicti155 – 171AAQKQ…SSGEA → LRKNKGSAASSTVLGQG in AAA24321 (PubMed:6235149).CuratedAdd BLAST17
Sequence conflicti245 – 246PV → AL in AAA24321 (PubMed:6235149).Curated2
Sequence conflicti257 – 258SM → RL in AAA24321 (PubMed:6235149).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
K02500 Genomic DNA Translation: AAA24321.1
U00096 Genomic DNA Translation: AAC74793.1
AP009048 Genomic DNA Translation: BAA15500.2
K00128 Genomic DNA Translation: AAA24320.1

Protein sequence database of the Protein Information Resource

More...PIRi		C64931, KIECFB

NCBI Reference Sequences

More...RefSeqi		NP_416237.3, NC_000913.3
WP_000251727.1, NZ_SSZK01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74793; AAC74793; b1723
BAA15500; BAA15500; BAA15500

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946230

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW5280
eco:b1723

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.533

<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
K02500 Genomic DNA Translation: AAA24321.1
U00096 Genomic DNA Translation: AAC74793.1
AP009048 Genomic DNA Translation: BAA15500.2
K00128 Genomic DNA Translation: AAA24320.1
PIRiC64931, KIECFB
RefSeqiNP_416237.3, NC_000913.3
WP_000251727.1, NZ_SSZK01000001.1

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
3CQDX-ray1.98A/B1-309[»]
3N1CX-ray2.00A/B/C/D1-309[»]
3UMOX-ray1.70A/B1-309[»]
3UMPX-ray1.85A/B1-309[»]
3UQDX-ray2.14A/B/C/D1-309[»]
3UQEX-ray2.20A/B1-309[»]
AlphaFoldDBiP06999
SMRiP06999
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263076, 25 interactors
DIPiDIP-10465N
MINTiP06999
STRINGi511145.b1723

2D gel databases

SWISS-2DPAGEiP06999

Proteomic databases

jPOSTiP06999
PaxDbiP06999
PRIDEiP06999

Genome annotation databases

EnsemblBacteriaiAAC74793; AAC74793; b1723
BAA15500; BAA15500; BAA15500
GeneIDi946230
KEGGiecj:JW5280
eco:b1723
PATRICifig|1411691.4.peg.533

Organism-specific databases

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

More...EchoBASEi		EB0694

Phylogenomic databases

eggNOGiCOG1105, Bacteria
HOGENOMiCLU_050013_0_2_6
InParanoidiP06999
OMAiQLNEPGP
PhylomeDBiP06999

Enzyme and pathway databases

UniPathwayiUPA00109;UER00182
BioCyciEcoCyc:6PFK-2-MONOMER
BRENDAi2.7.1.11, 2026
SABIO-RKiP06999

Miscellaneous databases

EvolutionaryTraceiP06999

Protein Ontology

More...PROi		PR:P06999

Family and domain databases

CDDicd01164, FruK_PfkB_like, 1 hit
Gene3Di3.40.1190.20, 1 hit
InterProiView protein in InterPro
IPR002173, Carboh/pur_kinase_PfkB_CS
IPR011611, PfkB_dom
IPR029056, Ribokinase-like
IPR017583, Tagatose/fructose_Pkinase
PfamiView protein in Pfam
PF00294, PfkB, 1 hit
PIRSFiPIRSF000535, 1PFK/6PFK/LacC, 1 hit
SUPFAMiSSF53613, SSF53613, 1 hit
TIGRFAMsiTIGR03168, 1-PFK, 1 hit
PROSITEiView protein in PROSITE
PS00583, PFKB_KINASES_1, 1 hit
PS00584, PFKB_KINASES_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiPFKB_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: P06999
Secondary accession number(s): P78065, P78260
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: May 25, 2022
This is version 179 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, 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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