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UniProtKB - P0A796 (PFKA_ECOLI)

Protein

ATP-dependent 6-phosphofructokinase isozyme 1

Gene

pfkA

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.UniRule annotation

<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 ‘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+UniRule annotation1 Publication

<p>This subsection of the ‘Function’ 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 ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation

<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: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA)
  4. Fructose-bisphosphate aldolase class 2 (fbaA)
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 ‘Function’ 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 sitei12ATP; via amide nitrogenUniRule annotation1 Publication1
<p>This subsection of the ‘Function’ 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 bindingi104Magnesium; catalyticUniRule annotation1 Publication1
<p>This subsection of the ‘Function’ 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 sitei128Proton acceptorUniRule annotation2 Publications1
Binding sitei155Allosteric activator ADPUniRule annotation1 Publication1
Binding sitei163Substrate; shared with dimeric partnerUniRule annotation1 Publication1
Binding sitei212Allosteric activator ADPUniRule annotationBy similarity1
Binding sitei223SubstrateUniRule annotation1 Publication1
Binding sitei244Substrate; shared with dimeric partnerUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi73 – 74ATPUniRule annotation1 Publication2
Nucleotide bindingi103 – 106ATPUniRule annotation1 Publication4

<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

  • 6-phosphofructokinase activity Source: EcoCyc
  • AMP binding Source: GO_Central
  • ATP binding Source: EcoliWiki
  • fructose-6-phosphate binding Source: GO_Central
  • GDP binding Source: EcoCyc
  • identical protein binding Source: EcoliWiki
  • magnesium ion binding Source: EcoliWiki
  • monosaccharide binding Source: GO_Central
  • ribonucleotide binding Source: EcoliWiki
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:6PFK-1-MONOMER
MetaCyc:6PFK-1-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.1.11 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A796

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_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:
ATP-dependent 6-phosphofructokinase isozyme 1UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 1UniRule annotation
Short name:
Phosphofructokinase 1UniRule annotation
Alternative name(s):
6-phosphofructokinase isozyme I
Phosphohexokinase 1UniRule annotation
<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:pfkAUniRule annotation
Ordered Locus Names:b3916, JW3887
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10699 pfkA

<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

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<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>Mutagenesisi128D → S: 18000-fold reduction of catalytic rate. 1 Publication1
Mutagenesisi172R → S: 3.4-fold reduction in turnover numbers. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001119501 – 320ATP-dependent 6-phosphofructokinase isozyme 1Add BLAST320

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A796

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

More...PaxDbi		P0A796

PRoteomics IDEntifications database

More...PRIDEi		P0A796

2D gel databases

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

More...SWISS-2DPAGEi		P0A796

<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.UniRule annotation1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4261224, 17 interactors

Database of interacting proteins

More...DIPi		DIP-35841N

Protein interaction database and analysis system

More...IntActi		P0A796, 7 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_4105

<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

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0A796

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

More...SMRi		P0A796

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A796

<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>Regioni22 – 26Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication5
Regioni55 – 60Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation1 Publication6
Regioni126 – 128Substrate bindingUniRule annotation1 Publication3
Regioni170 – 172Substrate bindingUniRule annotationBy similarity3
Regioni186 – 188Allosteric activator ADP bindingUniRule annotation1 Publication3
Regioni214 – 216Allosteric activator ADP bindingUniRule annotation1 Publication3
Regioni250 – 253Substrate bindingUniRule annotation1 Publication4

<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 phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CTQ Bacteria
COG0205 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000248870

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A796

KEGG Orthology (KO)

More...KOi		K00850

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A796

Family and domain databases

Conserved Domains Database

More...CDDi		cd00763 Bacterial_PFK, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00339 Phosphofructokinase_I_B1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR022953 ATP_PFK
IPR012003 ATP_PFK_prok-type
IPR012828 PFKA_ATP_prok
IPR015912 Phosphofructokinase_CS
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00365 PFK, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000532 ATP_PFK_prok, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00476 PHFRCTKINASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53784 SSF53784, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02482 PFKA_ATP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 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>.<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.

P0A796-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM 
        60         70         80         90        100
VQLDRYSVSD MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV 
       110        120        130        140        150
IGGDGSYMGA MRLTEMGFPC IGLPGTIDND IKGTDYTIGF FTALSTVVEA 
       160        170        180        190        200
IDRLRDTSSS HQRISVVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE 
       210        220        230        240        250
DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG RETRATVLGH 
       260        270        280        290        300
IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 
       310        320
IENMKRPFKG DWLDCAKKLY
Length:320
Mass (Da):34,842
Last modified:June 7, 2005 - v1
<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:iD03D79F6A5536A41
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 conflicti74F → C in CAA26356 (PubMed:3158524).Curated1
Sequence conflicti103 – 104GD → DG in CAA26356 (PubMed:3158524).Curated2
Sequence conflicti163R → P in CAA26356 (PubMed:3158524).Curated1
Sequence conflicti317 – 319KKL → EKM in CAA26356 (PubMed:3158524).Curated3

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
X02519 Genomic DNA Translation: CAA26356.1
L19201 Genomic DNA Translation: AAB03048.1
U00096 Genomic DNA Translation: AAC76898.1
AP009048 Genomic DNA Translation: BAE77394.1

Protein sequence database of the Protein Information Resource

More...PIRi		G65197 KIECFA

NCBI Reference Sequences

More...RefSeqi		NP_418351.1, NC_000913.3
WP_000591795.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76898; AAC76898; b3916
BAE77394; BAE77394; BAE77394

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948412

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3887
eco:b3916

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2789

<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
X02519 Genomic DNA Translation: CAA26356.1
L19201 Genomic DNA Translation: AAB03048.1
U00096 Genomic DNA Translation: AAC76898.1
AP009048 Genomic DNA Translation: BAE77394.1
PIRiG65197 KIECFA
RefSeqiNP_418351.1, NC_000913.3
WP_000591795.1, NZ_LN832404.1

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
1PFKX-ray2.40A/B1-320[»]
2PFKX-ray2.40A/B/C/D1-320[»]
ProteinModelPortaliP0A796
SMRiP0A796
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261224, 17 interactors
DIPiDIP-35841N
IntActiP0A796, 7 interactors
STRINGi316385.ECDH10B_4105

2D gel databases

SWISS-2DPAGEiP0A796

Proteomic databases

EPDiP0A796
PaxDbiP0A796
PRIDEiP0A796

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76898; AAC76898; b3916
BAE77394; BAE77394; BAE77394
GeneIDi948412
KEGGiecj:JW3887
eco:b3916
PATRICifig|1411691.4.peg.2789

Organism-specific databases

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

More...EchoBASEi		EB0693
EcoGeneiEG10699 pfkA

Phylogenomic databases

eggNOGiENOG4105CTQ Bacteria
COG0205 LUCA
HOGENOMiHOG000248870
InParanoidiP0A796
KOiK00850
PhylomeDBiP0A796

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

BioCyciEcoCyc:6PFK-1-MONOMER
MetaCyc:6PFK-1-MONOMER
BRENDAi2.7.1.11 2026
SABIO-RKiP0A796

Miscellaneous databases

EvolutionaryTraceiP0A796

Protein Ontology

More...PROi		PR:P0A796

Family and domain databases

CDDicd00763 Bacterial_PFK, 1 hit
HAMAPiMF_00339 Phosphofructokinase_I_B1, 1 hit
InterProiView protein in InterPro
IPR022953 ATP_PFK
IPR012003 ATP_PFK_prok-type
IPR012828 PFKA_ATP_prok
IPR015912 Phosphofructokinase_CS
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf
PfamiView protein in Pfam
PF00365 PFK, 1 hit
PIRSFiPIRSF000532 ATP_PFK_prok, 1 hit
PRINTSiPR00476 PHFRCTKINASE
SUPFAMiSSF53784 SSF53784, 1 hit
TIGRFAMsiTIGR02482 PFKA_ATP, 1 hit
PROSITEiView protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiPFKA_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: P0A796
Secondary accession number(s): P06998, Q2M8L2
<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: April 1, 1988
Last sequence update: June 7, 2005
Last modified: December 5, 2018
This is version 120 of the entry and version 1 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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