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Entry version 99 (26 Feb 2020)
Sequence version 1 (01 Nov 1996)
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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

Gene
N/A
Organism
Lithobates catesbeianus (American bullfrog) (Rana catesbeiana)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

Synthesis and degradation of fructose 2,6-bisphosphate.

<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 <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

Phosphorylation results in inhibition of the kinase activity.By similarity

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 sitei80Fructose 6-phosphateBy similarity1
Binding sitei104Fructose 6-phosphateBy similarity1
<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 sitei130Sequence analysis1
Binding sitei132Fructose 6-phosphateBy similarity1
Binding sitei138Fructose 6-phosphateBy similarity1
Active sitei160Sequence analysis1
Binding sitei174Fructose 6-phosphateBy similarity1
Binding sitei195Fructose 6-phosphateBy similarity1
Binding sitei199Fructose 6-phosphateBy similarity1
Binding sitei257Fructose 2,6-bisphosphateBy similarity1
<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>Sitei257Transition state stabilizerBy similarity1
Active sitei258Tele-phosphohistidine intermediateBy similarity1
Binding sitei264Fructose 2,6-bisphosphateBy similarity1
Sitei264Transition state stabilizerBy similarity1
Binding sitei270Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei327Proton donor/acceptorBy similarity1
Binding sitei338Fructose 2,6-bisphosphateBy similarity1
Binding sitei352Fructose 2,6-bisphosphateBy similarity1
Binding sitei356Fructose 2,6-bisphosphateBy similarity1
Binding sitei367Fructose 2,6-bisphosphateBy similarity1
Sitei392Transition state stabilizerBy similarity1
Binding sitei393Fructose 2,6-bisphosphateBy similarity1
Binding sitei397Fructose 2,6-bisphosphateBy similarity1
Binding sitei429ATPBy similarity1

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 bindingi47 – 55ATPBy similarity9
Nucleotide bindingi169 – 174ATPBy similarity6
Nucleotide bindingi349 – 352ATPBy similarity4
Nucleotide bindingi393 – 397ATPBy similarity5

<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 functionHydrolase, Kinase, Multifunctional enzyme, Transferase
LigandATP-binding, Nucleotide-binding

<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:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Short name:
6PF-2-K/Fru-2,6-P2ase
Short name:
PFK/FBPase
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver/muscle isozymes
Including the following 2 domains:
6-phosphofructo-2-kinase (EC:2.7.1.105)
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
<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>OrganismiLithobates catesbeianus (American bullfrog) (Rana catesbeiana)
<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 identifieri8400 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeLithobates

<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_00001799731 – 4706-phosphofructo-2-kinase/fructose-2,6-bisphosphataseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei31Phosphoserine; by PKABy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q91309

<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.

By similarity

<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

3D structure databases

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

More...
SMRi
Q91309

Database of comparative protein structure models

More...
ModBasei
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>Regioni1 – 2496-phosphofructo-2-kinaseAdd BLAST249
Regioni250 – 470Fructose-2,6-bisphosphataseAdd BLAST221

<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

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07067 HP_PGM_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1240, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10606 PTHR10606, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00991 6PFRUCTKNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00855 PGAM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00175 PG_MUTASE, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform Liver (identifier: Q91309-1) [UniParc]FASTAAdd to basket
Also known as: L-type

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MADRLRELTQ TRLQKIWIPH QCDRLQQRRG SSIPQFTNSP TMIVMVGLPA
60 70 80 90 100
RGKTYISKKL TRYLNWIGTP TKVFNVGQYR RDATQSYNNY QFFRADNQEA
110 120 130 140 150
MKIRKQCALH ALKDVHTYLS REEGHVAVFD ATNTTRERRS VILQFAKERG
160 170 180 190 200
YKVFFIESIC DDPDIIAENI TQVKLSSPDY TGCDREKVLE DFLKRIDCYQ
210 220 230 240 250
MNYEPLHDDL DSSLSYIKIF NVGSRYLVNR VQDHIQSRAV YYLMNIHVTP
260 270 280 290 300
RSIYLSRHGE SELNLLGRIG GDSGLSVRGK QYAHELGNFI KSQQIPDLKV
310 320 330 340 350
WTSHMKRTIQ TAEALHVPYE QWKALNEIDA GVCEEMTYEE IQDHFPEEFA
360 370 380 390 400
LRDQDKYRYR YPKGESYEDI VQRLEPVIME LERQENVLVI CHQAVMRCLL
410 420 430 440 450
AYFLDKTAEE LPYLKCPLHT VLKLTPVAYG CKVESIYLNI EAVNTHREKP
460 470
LNVEVSRDPE EALDTVPEHF
Length:470
Mass (Da):54,933
Last modified:November 1, 1996 - 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:i53112EF3B886D310
GO
Isoform Muscle (identifier: Q91309-2) [UniParc]FASTAAdd to basket
Also known as: M-type

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MADRLRELTQTRLQKIWIPHQCDRLQQRRGS → MEGNYKLLEDKASRIPA

Show »
Length:456
Mass (Da):53,033
Checksum:i82472C3EC856AEC5
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0046851 – 31MADRL…QRRGS → MEGNYKLLEDKASRIPA in isoform Muscle. 1 PublicationAdd BLAST31

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
D25223 mRNA Translation: BAA04952.1
D25222 mRNA Translation: BAA04951.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC2064

Keywords - Coding sequence diversityi

Alternative splicing

<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
D25223 mRNA Translation: BAA04952.1
D25222 mRNA Translation: BAA04951.1
PIRiJC2064

3D structure databases

SMRiQ91309
ModBaseiSearch...

Proteomic databases

PRIDEiQ91309

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS
PANTHERiPTHR10606 PTHR10606, 1 hit
PfamiView protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit
PRINTSiPR00991 6PFRUCTKNASE
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiF26_LITCT
<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: Q91309
Secondary accession number(s): Q91310
<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: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 26, 2020
This is version 99 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 programChordata 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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