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Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

Pfkl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (PubMed:26194095).UniRule annotation1 Publication

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Activity regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation (By similarity).UniRule annotation

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 (Gpi), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gpi1)
  3. ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase (Aldob), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (Aldob), Fructose-bisphosphate aldolase (Aldoart1)
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
Binding sitei25ATP; via amide nitrogenUniRule annotation1
Metal bindingi119Magnesium; catalyticUniRule annotation1
Active sitei166Proton acceptorUniRule annotation1
Binding sitei201Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Binding sitei292Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei470Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei565Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei628Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei654Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei734Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 89ATPUniRule annotation2
Nucleotide bindingi118 – 121ATPUniRule annotation4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: MGI
  • AMP binding Source: GO_Central
  • ATP binding Source: MGI
  • fructose-6-phosphate binding Source: MGI
  • fructose binding Source: MGI
  • identical protein binding Source: MGI
  • kinase binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • monosaccharide binding Source: MGI

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-6798695 Neutrophil degranulation
R-MMU-70171 Glycolysis
SABIO-RKiP12382
UniPathwayi
UPA00109;UER00182

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, liver typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-L
Alternative name(s):
6-phosphofructokinase type B
Phosphofructo-1-kinase isozyme B
Short name:
PFK-B
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PfklImported
Synonyms:Pfk-l, Pfkb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97547 Pfkl

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001120222 – 780ATP-dependent 6-phosphofructokinase, liver typeAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei377PhosphoserineBy similarity1
Glycosylationi529O-linked (GlcNAc) serineBy similarity1
Modified residuei640PhosphotyrosineCombined sources1
Modified residuei775PhosphoserineCombined sources1

Post-translational modificationi

GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP12382
MaxQBiP12382
PaxDbiP12382
PeptideAtlasiP12382
PRIDEiP12382

PTM databases

iPTMnetiP12382
PhosphoSitePlusiP12382
SwissPalmiP12382

Expressioni

Gene expression databases

BgeeiENSMUSG00000020277 Expressed in 347 organ(s), highest expression level in stria vascularis of cochlear duct
CleanExiMM_PFKL
ExpressionAtlasiP12382 baseline and differential
GenevisibleiP12382 MM

Interactioni

Subunit structurei

Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable).UniRule annotationCurated

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202124, 6 interactors
ComplexPortaliCPX-2052 6-phosphofructokinase, L4 homotetramer
CPX-2055 6-phosphofructokinase, ML3 heterotetramer
CPX-2056 6-phosphofructokinase, M2L2 heterotetramer
CPX-2057 6-phosphofructokinase, M3L heterotetramer
IntActiP12382, 10 interactors
MINTiP12382
STRINGi10090.ENSMUSP00000020522

Structurei

3D structure databases

ProteinModelPortaliP12382
SMRiP12382
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 390N-terminal catalytic PFK domain 1Add BLAST389
Regioni164 – 166Substrate bindingUniRule annotation3
Regioni208 – 210Substrate bindingUniRule annotation3
Regioni298 – 301Substrate bindingUniRule annotation4
Regioni391 – 400Interdomain linker10
Regioni401 – 780C-terminal regulatory PFK domain 2Add BLAST380
Regioni527 – 531Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni572 – 574Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni660 – 663Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
GeneTreeiENSGT00390000013209
HOGENOMiHOG000200154
HOVERGENiHBG000976
InParanoidiP12382
KOiK00850
OMAiDPFNIQD
OrthoDBiEOG091G01YN
TreeFamiTF300411

Family and domain databases

HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
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
TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 2 hits

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P12382-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL
60 70 80 90 100
IYEGYEGLVE GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA
110 120 130 140 150
AAYNLLQHGI TNLCVIGGDG SLTGANIFRN EWGSLLEELV KEGKISESTA
160 170 180 190 200
QNYAHLTIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET
260 270 280 290 300
RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME
360 370 380 390 400
CVQVTKDVQK AMDEERFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF
410 420 430 440 450
SLAILNVGAP AAGMNAAVRS AVRTGISEGH TVYIVHDGFE GLAKGQVQEV
460 470 480 490 500
GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI VENLRTYNIH ALLVIGGFEA
510 520 530 540 550
YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME
560 570 580 590 600
SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
610 620 630 640 650
IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV
660 670 680 690 700
FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWVSEKL RDVYRKGRVF
710 720 730 740 750
ANAPDSACVI GLRKKVVAFS PVTELKKETD FEHRMPREQW WLNLRLMLKM
760 770 780
LAHYRISMAD YVSGELEHVT RRTLSIDKGF
Length:780
Mass (Da):85,360
Last modified:July 27, 2011 - v4
Checksum:i0C12E2C222020B7F
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1W2P7T1A0A1W2P7T1_MOUSE
ATP-dependent 6-phosphofructokinase...
Pfkl
167Annotation score:
A0A1W2P6Q4A0A1W2P6Q4_MOUSE
ATP-dependent 6-phosphofructokinase...
Pfkl
64Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti419R → P in AAA20076 (PubMed:2969893).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03928 mRNA Translation: AAA20076.1
AK030511 mRNA Translation: BAC26997.1
AK036318 mRNA Translation: BAC29382.1
AK081313 mRNA Translation: BAC38193.1
AK159328 mRNA Translation: BAE34994.1
CH466553 Genomic DNA Translation: EDL31763.1
BC020097 mRNA Translation: AAH20097.1
CCDSiCCDS35955.1
PIRiA31070
RefSeqiNP_032852.2, NM_008826.4
UniGeneiMm.269649

Genome annotation databases

EnsembliENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277
GeneIDi18641
KEGGimmu:18641
UCSCiuc007fwo.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03928 mRNA Translation: AAA20076.1
AK030511 mRNA Translation: BAC26997.1
AK036318 mRNA Translation: BAC29382.1
AK081313 mRNA Translation: BAC38193.1
AK159328 mRNA Translation: BAE34994.1
CH466553 Genomic DNA Translation: EDL31763.1
BC020097 mRNA Translation: AAH20097.1
CCDSiCCDS35955.1
PIRiA31070
RefSeqiNP_032852.2, NM_008826.4
UniGeneiMm.269649

3D structure databases

ProteinModelPortaliP12382
SMRiP12382
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202124, 6 interactors
ComplexPortaliCPX-2052 6-phosphofructokinase, L4 homotetramer
CPX-2055 6-phosphofructokinase, ML3 heterotetramer
CPX-2056 6-phosphofructokinase, M2L2 heterotetramer
CPX-2057 6-phosphofructokinase, M3L heterotetramer
IntActiP12382, 10 interactors
MINTiP12382
STRINGi10090.ENSMUSP00000020522

PTM databases

iPTMnetiP12382
PhosphoSitePlusiP12382
SwissPalmiP12382

Proteomic databases

EPDiP12382
MaxQBiP12382
PaxDbiP12382
PeptideAtlasiP12382
PRIDEiP12382

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277
GeneIDi18641
KEGGimmu:18641
UCSCiuc007fwo.2 mouse

Organism-specific databases

CTDi5211
MGIiMGI:97547 Pfkl

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
GeneTreeiENSGT00390000013209
HOGENOMiHOG000200154
HOVERGENiHBG000976
InParanoidiP12382
KOiK00850
OMAiDPFNIQD
OrthoDBiEOG091G01YN
TreeFamiTF300411

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

ReactomeiR-MMU-6798695 Neutrophil degranulation
R-MMU-70171 Glycolysis
SABIO-RKiP12382

Miscellaneous databases

PROiPR:P12382
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020277 Expressed in 347 organ(s), highest expression level in stria vascularis of cochlear duct
CleanExiMM_PFKL
ExpressionAtlasiP12382 baseline and differential
GenevisibleiP12382 MM

Family and domain databases

HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
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
TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiPFKAL_MOUSE
AccessioniPrimary (citable) accession number: P12382
Secondary accession number(s): Q8VDX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 175 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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