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Entry version 209 (29 Sep 2021)
Sequence version 4 (23 Jan 2007)
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Protein

ATP-dependent 6-phosphofructokinase subunit beta

Gene

PFK2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 annotation8 Publications

Miscellaneous

Present with 90200 molecules/cell in log phase SD medium.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 '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 annotation

<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 ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation3 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=0.24 mM for ATP (without effector)1 Publication
  2. KM=0.3 mM for ATP (with 1 mM AMP)1 Publication
  3. KM=0.31 mM for ATP (with 20 µM fructose 2,6-bisphosphate)1 Publication
  4. KM=1.65 mM for fructose 6-phosphate (without effector)1 Publication
  5. KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
  6. KM=0.11 mM for fructose 6-phosphate (with 20 µM fructose 2,6-bisphosphate)1 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: 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 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_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 sitei206ATP; via amide nitrogenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi301Magnesium; catalyticUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei348Proton acceptorUniRule annotation1
Binding sitei383Substrate; shared with subunit alphaUniRule annotation1 Publication1
Binding sitei447SubstrateUniRule annotation1 Publication1
Binding sitei475Substrate; shared with subunit alphaUniRule annotation1 Publication1
Binding sitei658Fructose 2,6-bisphosphate; allosteric activatorUniRule annotation1 Publication1
Binding sitei754Fructose 2,6-bisphosphate; allosteric activator; shared with subunit alphaUniRule annotation1
Binding sitei847Fructose 2,6-bisphosphate; allosteric activator; shared with subunit alphaUniRule annotation1
Binding sitei935Fructose 2,6-bisphosphate; allosteric activatorUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi270 – 271ATPUniRule annotation2
Nucleotide bindingi300 – 303ATPUniRule annotation4

<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, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YMR205C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.11, 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-6798695, Neutrophil degranulation
R-SCE-70171, Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P16862

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 subunit betaUniRule annotation (EC:2.7.1.11UniRule annotation)
Alternative name(s):
ATP-dependent 6-phosphofructokinaseUniRule annotation
Short name:
ATP-PFKUniRule annotation
Short name:
Phosphofructokinase 2UniRule annotation
PhosphohexokinaseUniRule 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:PFK2
Ordered Locus Names:YMR205C
ORF Names:YM8325.06C
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004818, PFK2

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YMR205C

<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

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

<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>Mutagenesisi301D → T: Reduces maximal activity of the holoenzyme by 30%. 1 Publication1
Mutagenesisi348D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'T-309' or 'S-356' in subunit alpha. 1 Publication1
Mutagenesisi439R → V: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication1
Mutagenesisi481H → S: Increases the KM for fructose 6-phosphate 50 fold. 1 Publication1
Mutagenesisi718S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-724' in subunit alpha. 1 Publication1
Mutagenesisi722P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication1
Mutagenesisi853H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-859' in subunit alpha. 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 methionineiRemoved1 Publication
<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_00001120462 – 959ATP-dependent 6-phosphofructokinase subunit betaAdd BLAST958

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 residuei152PhosphothreonineCombined sources1
Modified residuei163PhosphoserineCombined sources1
Modified residuei171PhosphoserineCombined sources1
Modified residuei803PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P16862

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

More...
PaxDbi
P16862

PRoteomics IDEntifications database

More...
PRIDEi
P16862

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P16862

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16862

<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

Heterooctamer of 4 alpha and 4 beta chains.

UniRule annotation3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35383, 407 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-554, 6-phosphofructokinase complex

Database of interacting proteins

More...
DIPi
DIP-2619N

Protein interaction database and analysis system

More...
IntActi
P16862, 104 interactors

Molecular INTeraction database

More...
MINTi
P16862

STRING: functional protein association networks

More...
STRINGi
4932.YMR205C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P16862, protein

<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

1959
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
P16862

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>Regioni2 – 573N-terminal catalytic PFK domain 1UniRule annotation1 PublicationAdd BLAST572
Regioni144 – 167DisorderedSequence analysisAdd BLAST24
Regioni346 – 348Substrate bindingUniRule annotation1 Publication3
Regioni390 – 392Substrate bindingUniRule annotation1 Publication3
Regioni481 – 484Substrate bindingUniRule annotation1 Publication4
Regioni574 – 587Interdomain linkerUniRule annotation1 PublicationAdd BLAST14
Regioni588 – 959C-terminal regulatory PFK domain 2UniRule annotation1 PublicationAdd BLAST372
Regioni716 – 720Fructose 2,6-bisphosphate binding; allosteric activatorUniRule annotation1 Publication5
Regioni761 – 763Fructose 2,6-bisphosphate binding; allosteric activatorUniRule annotation1 Publication3
Regioni853 – 856Fructose 2,6-bisphosphate binding; allosteric activatorUniRule 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2440, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000171778

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011053_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16862

Identification of Orthologs from Complete Genome Data

More...
OMAi
GTPCAYD

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.180.10, 1 hit
3.40.50.460, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_03184, Phosphofructokinase_I_E, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009161, 6-Pfructokinase_euk
IPR022953, ATP_PFK
IPR029068, Glyas_Bleomycin-R_OHBP_Dase
IPR015912, Phosphofructokinase_CS
IPR000023, Phosphofructokinase_dom
IPR035966, PKF_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00365, PFK, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000533, ATP_PFK_euk, 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, 2 hits
SSF54593, SSF54593, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02478, 6PF1K_euk, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00433, PHOSPHOFRUCTOKINASE, 2 hits

<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.

P16862-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL
60 70 80 90 100
SNDSISLKIL LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS
110 120 130 140 150
DILAVKDTLN AMNAPLQGYP TELFPMQLYT LDPLGNVVGV TSTKNAVSTK
160 170 180 190 200
PTPPPAPEAS AESGLSSKVH SYTDLAYRMK TTDTYPSLPK PLNRPQKAIA
210 220 230 240 250
VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV RGGPEYIKEF
260 270 280 290 300
HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG
310 320 330 340 350
DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND
360 370 380 390 400
MSTTDATIGA YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL
410 420 430 440 450
AGIATSADYI FIPEKPATSS EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI
460 470 480 490 500
AADLTPISPS DVHKVLVDRL GLDTRITTLG HVQRGGTAVA YDRILATLQG
510 520 530 540 550
LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA VAEAIQAKDF
560 570 580 590 600
KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG
610 620 630 640 650
INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG
660 670 680 690 700
GSEIGTNRVT PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR
710 720 730 740 750
ESYPAFRIPM VLIPATLSNN VPGTEYSLGS DTALNALMEY CDVVKQSASS
760 770 780 790 800
TRGRAFVVDC QGGNSGYLAT YASLAVGAQV SYVPEEGISL EQLSEDIEYL
810 820 830 840 850
AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA DGRFDAKPAY
860 870 880 890 900
PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD
910 920 930 940 950
KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD

HLVGRKRVD
Length:959
Mass (Da):104,618
Last modified:January 23, 2007 - v4
<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:i82CE6402CEDBBCB2
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 conflicti137V → G in AAA34860 (PubMed:2528496).Curated1
Sequence conflicti880K → E in AAA34860 (PubMed:2528496).Curated1

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
M26944 Genomic DNA Translation: AAA34860.1
Z48755 Genomic DNA Translation: CAA88646.1
BK006946 Genomic DNA Translation: DAA10104.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S59446, JQ0017

NCBI Reference Sequences

More...
RefSeqi
NP_013932.1, NM_001182712.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR205C_mRNA; YMR205C; YMR205C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855245

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR205C

<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
M26944 Genomic DNA Translation: AAA34860.1
Z48755 Genomic DNA Translation: CAA88646.1
BK006946 Genomic DNA Translation: DAA10104.1
PIRiS59446, JQ0017
RefSeqiNP_013932.1, NM_001182712.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O8OX-ray2.90B/D/F/H194-959[»]
SMRiP16862
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35383, 407 interactors
ComplexPortaliCPX-554, 6-phosphofructokinase complex
DIPiDIP-2619N
IntActiP16862, 104 interactors
MINTiP16862
STRINGi4932.YMR205C

PTM databases

CarbonylDBiP16862
iPTMnetiP16862

Proteomic databases

MaxQBiP16862
PaxDbiP16862
PRIDEiP16862

Genome annotation databases

EnsemblFungiiYMR205C_mRNA; YMR205C; YMR205C
GeneIDi855245
KEGGisce:YMR205C

Organism-specific databases

SGDiS000004818, PFK2
VEuPathDBiFungiDB:YMR205C

Phylogenomic databases

eggNOGiKOG2440, Eukaryota
GeneTreeiENSGT00940000171778
HOGENOMiCLU_011053_0_0_1
InParanoidiP16862
OMAiGTPCAYD

Enzyme and pathway databases

UniPathwayiUPA00109;UER00182
BioCyciMetaCyc:YMR205C-MONOMER
BRENDAi2.7.1.11, 984
ReactomeiR-SCE-6798695, Neutrophil degranulation
R-SCE-70171, Glycolysis
SABIO-RKiP16862

Miscellaneous databases

Protein Ontology

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PROi
PR:P16862
RNActiP16862, protein

Family and domain databases

Gene3Di3.10.180.10, 1 hit
3.40.50.460, 2 hits
HAMAPiMF_03184, Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161, 6-Pfructokinase_euk
IPR022953, ATP_PFK
IPR029068, Glyas_Bleomycin-R_OHBP_Dase
IPR015912, Phosphofructokinase_CS
IPR000023, Phosphofructokinase_dom
IPR035966, PKF_sf
PfamiView protein in Pfam
PF00365, PFK, 2 hits
PIRSFiPIRSF000533, ATP_PFK_euk, 1 hit
PRINTSiPR00476, PHFRCTKINASE
SUPFAMiSSF53784, SSF53784, 2 hits
SSF54593, SSF54593, 1 hit
TIGRFAMsiTIGR02478, 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433, PHOSPHOFRUCTOKINASE, 2 hits

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 nameiPFKA2_YEAST
<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: P16862
Secondary accession number(s): D6W030
<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: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 209 of the entry and version 4 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 programFungal 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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