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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

Pfkm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.UniRule annotation1 Publication

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation1 Publication

Cofactori

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.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, liver type (Pfkl), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm)
  4. Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldob), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase (Aldob)
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 sitei471Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei566Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei629Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei655Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei735Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

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

GO - Molecular functioni

GO - Biological processi

  • canonical glycolysis Source: MGI
  • fructose 6-phosphate metabolic process Source: MGI
  • glucose homeostasis Source: MGI
  • glycogen catabolic process Source: MGI
  • glycolysis from storage polysaccharide through glucose-1-phosphate Source: MGI
  • glycolytic process Source: MGI
  • glycolytic process through fructose-6-phosphate Source: MGI
  • muscle cell cellular homeostasis Source: MGI
  • positive regulation of insulin secretion Source: MGI
  • protein oligomerization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-70171. Glycolysis.
SABIO-RKP47857.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
PhosphohexokinaseUniRule annotation
Gene namesi
Name:Pfkm
Synonyms:Pfk-m, Pfka
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:97548. Pfkm.

Subcellular locationi

  • Cytoplasm UniRule annotation
Isoform 2 :
  • Cell projectionciliumflagellum 1 Publication

  • Note: Principal piece region of the sperm flagellum.1 Publication
Isoform 3 :
  • Cell projectionciliumflagellum 1 Publication

  • Note: Principal piece region of the sperm flagellum.1 Publication

GO - Cellular componenti

  • 6-phosphofructokinase complex Source: MGI
  • apical plasma membrane Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • sperm principal piece Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Flagellum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001120182 – 780ATP-dependent 6-phosphofructokinase, muscle typeAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei133PhosphoserineBy similarity1
Modified residuei377PhosphoserineCombined sources1
Glycosylationi530O-linked (GlcNAc)By similarity1
Modified residuei667PhosphoserineBy similarity1
Modified residuei775PhosphoserineBy similarity1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP47857.
MaxQBiP47857.
PaxDbiP47857.
PeptideAtlasiP47857.
PRIDEiP47857.

PTM databases

iPTMnetiP47857.
PhosphoSitePlusiP47857.
SwissPalmiP47857.

Miscellaneous databases

PMAP-CutDBP47857.

Expressioni

Tissue specificityi

Isoform 1 is expressed in skeletal muscle (at protein level). Isoform 2 and isoform 3 are testis-specific and are detected in quiescent sperm (at protein level). They are first detected in the cytoplasm of round spermatids and subsequently in the flagellum of elongated spermatids extending into the seminiferous tubule lumen (at protein level). Isoform 2 is expressed at higher level than isoform 3 in testis.1 Publication

Developmental stagei

Isoform 2 and isoform 3 are first seen on postnatal day 16 corresponding to the age when midpachytene spermatocytes are present in the synchronous first wave of spermatogenesis. Isoform 2 and isoform 3 levels increase substantially between days 14 and 18 and continue to increase to age 30 days of neonatal testis development.1 Publication

Gene expression databases

BgeeiENSMUSG00000033065.
CleanExiMM_PFKM.
GenevisibleiP47857. MM.

Interactioni

Subunit structurei

Homo- and heterotetramers. Isoform 2 and isoform 3 interact (via N-terminal testis-specific region) with GSTM5. Isoform 2 and isoform 3 interact (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region).1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202125. 2 interactors.
IntActiP47857. 4 interactors.
MINTiMINT-1869891.
STRINGi10090.ENSMUSP00000059801.

Structurei

3D structure databases

ProteinModelPortaliP47857.
SMRiP47857.
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 – 401Interdomain linkerAdd BLAST11
Regioni402 – 780C-terminal regulatory PFK domain 2Add BLAST379
Regioni528 – 532Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni573 – 575Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni661 – 664Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47857.
KOiK00850.
OMAiIFIPEMP.
OrthoDBiEOG091G01YN.
PhylomeDBiP47857.
TreeFamiTF300411.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47857-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF
60 70 80 90 100
VHEGYQGLVD GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLNDLQ KDGKITAEEA
160 170 180 190 200
TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIVEIVD AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET
260 270 280 290 300
RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME
360 370 380 390 400
CVQVTKDVTK AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL
410 420 430 440 450
HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE
460 470 480 490 500
AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ ISANITKFNI QGLVIIGGFE
510 520 530 540 550
AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI GADTALNTIC
560 570 580 590 600
TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
610 620 630 640 650
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG
660 670 680 690 700
IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVTELKDQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
Length:780
Mass (Da):85,269
Last modified:January 23, 2007 - v3
Checksum:i7917C7AC108B25C7
GO
Isoform 2 (identifier: P47857-2) [UniParc]FASTAAdd to basket
Also known as: Pfkms_V41 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRREEFQLRFFMCVIESRQVVRTTQSTAGEASTSNMTIPESKADDQWRLDGMDDDPSTVGPVSIPDTEWIM

Show »
Length:850
Mass (Da):93,248
Checksum:i054BC0B487ACDE63
GO
Isoform 3 (identifier: P47857-3) [UniParc]FASTAAdd to basket
Also known as: Pfkms_V31 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEEKLTCSFK...VSIPDTEWIM

Show »
Length:931
Mass (Da):102,384
Checksum:iDB9962A8A731FC77
GO

Sequence cautioni

The sequence AK138788 differs from that shown. Intron retention.1 Publication

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0570791M → MRREEFQLRFFMCVIESRQV VRTTQSTAGEASTSNMTIPE SKADDQWRLDGMDDDPSTVG PVSIPDTEWIM in isoform 2. 1 Publication1
Alternative sequenceiVSP_0570801M → MEEKLTCSFKLLTELLNLIT PLAQALFGKRLQNSILDPGD CLSEFTLEERKASGICQPHL FSKHKEINLFLQGILTCYEV AMRREEFQLRFFMCVIESRQ VVRTTQSTAGEASTSNMTIP ESKADDQWRLDGMDDDPSTV GPVSIPDTEWIM in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249894 mRNA. Translation: AAF63762.1.
AK002711 mRNA. Translation: BAB22303.1.
AK049773 mRNA. Translation: BAC33913.1.
AK138788 mRNA. No translation available.
D21864 Genomic DNA. Translation: BAA21892.1.
D21865 mRNA. Translation: BAA21012.1.
GQ428204 mRNA. Translation: ACU65458.1.
GQ428205 mRNA. Translation: ACU65459.1.
GQ428206 mRNA. Translation: ACU65460.1.
CCDSiCCDS27786.1. [P47857-1]
PIRiS53317.
RefSeqiNP_001156959.1. NM_001163487.1. [P47857-1]
NP_001156960.1. NM_001163488.1. [P47857-1]
NP_067489.3. NM_021514.4. [P47857-1]
XP_006520664.1. XM_006520601.3. [P47857-2]
XP_006520665.1. XM_006520602.2. [P47857-1]
UniGeneiMm.272582.
Mm.384023.

Genome annotation databases

EnsembliENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065. [P47857-1]
ENSMUST00000163507; ENSMUSP00000132803; ENSMUSG00000033065. [P47857-1]
GeneIDi18642.
KEGGimmu:18642.
UCSCiuc007xlv.2. mouse. [P47857-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249894 mRNA. Translation: AAF63762.1.
AK002711 mRNA. Translation: BAB22303.1.
AK049773 mRNA. Translation: BAC33913.1.
AK138788 mRNA. No translation available.
D21864 Genomic DNA. Translation: BAA21892.1.
D21865 mRNA. Translation: BAA21012.1.
GQ428204 mRNA. Translation: ACU65458.1.
GQ428205 mRNA. Translation: ACU65459.1.
GQ428206 mRNA. Translation: ACU65460.1.
CCDSiCCDS27786.1. [P47857-1]
PIRiS53317.
RefSeqiNP_001156959.1. NM_001163487.1. [P47857-1]
NP_001156960.1. NM_001163488.1. [P47857-1]
NP_067489.3. NM_021514.4. [P47857-1]
XP_006520664.1. XM_006520601.3. [P47857-2]
XP_006520665.1. XM_006520602.2. [P47857-1]
UniGeneiMm.272582.
Mm.384023.

3D structure databases

ProteinModelPortaliP47857.
SMRiP47857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202125. 2 interactors.
IntActiP47857. 4 interactors.
MINTiMINT-1869891.
STRINGi10090.ENSMUSP00000059801.

PTM databases

iPTMnetiP47857.
PhosphoSitePlusiP47857.
SwissPalmiP47857.

Proteomic databases

EPDiP47857.
MaxQBiP47857.
PaxDbiP47857.
PeptideAtlasiP47857.
PRIDEiP47857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065. [P47857-1]
ENSMUST00000163507; ENSMUSP00000132803; ENSMUSG00000033065. [P47857-1]
GeneIDi18642.
KEGGimmu:18642.
UCSCiuc007xlv.2. mouse. [P47857-1]

Organism-specific databases

CTDi5213.
MGIiMGI:97548. Pfkm.

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47857.
KOiK00850.
OMAiIFIPEMP.
OrthoDBiEOG091G01YN.
PhylomeDBiP47857.
TreeFamiTF300411.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
ReactomeiR-MMU-70171. Glycolysis.
SABIO-RKP47857.

Miscellaneous databases

ChiTaRSiPfkm. mouse.
PMAP-CutDBP47857.
PROiP47857.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000033065.
CleanExiMM_PFKM.
GenevisibleiP47857. MM.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKAM_MOUSE
AccessioniPrimary (citable) accession number: P47857
Secondary accession number(s): C8CMN5
, C8CMN6, C8CMN7, O35513, Q543L1, Q9JK94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.