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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

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)
  3. ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP)
  4. Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (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 sitei24ATP; via amide nitrogenUniRule annotation1
Metal bindingi118Magnesium; catalyticUniRule annotation1
Active sitei165Proton acceptorUniRule annotation1
Binding sitei200Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Binding sitei291Substrate; 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 bindingi87 – 88ATPUniRule annotation2
Nucleotide bindingi117 – 120ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-BTA-70171 Glycolysis
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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Organism-specific databases

VGNCiVGNC:32774 PFKM

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_00002844382 – 779ATP-dependent 6-phosphofructokinase, muscle typeAdd BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei376PhosphoserineBy similarity1
Glycosylationi529O-linked (GlcNAc) serineBy similarity1
Modified residuei666PhosphoserineBy similarity1
Modified residuei774PhosphoserineBy similarity1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ0IIG5
PeptideAtlasiQ0IIG5
PRIDEiQ0IIG5

Expressioni

Gene expression databases

BgeeiENSBTAG00000000286

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). Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).UniRule annotationBy similarityCurated

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000359

Structurei

3D structure databases

ProteinModelPortaliQ0IIG5
SMRiQ0IIG5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 389N-terminal catalytic PFK domain 1Add BLAST388
Regioni163 – 165Substrate bindingUniRule annotation3
Regioni207 – 209Substrate bindingUniRule annotation3
Regioni297 – 300Substrate bindingUniRule annotation4
Regioni390 – 400Interdomain linkerAdd BLAST11
Regioni401 – 779C-terminal regulatory PFK domain 2Add BLAST379
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

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
InParanoidiQ0IIG5
KOiK00850
OMAiKQYDELC
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

Sequencei

Sequence statusi: Complete.

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

Q0IIG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHEHHAAKT LGIGKAIAVL TSGGDAQGMN AAVRAVVRVG IYTGARVFFV
60 70 80 90 100
HEGYQGLVDG GDNIREATWE SVSMMLQLGG TVIGSARCKD FREREGRLRA
110 120 130 140 150
AHNLVKRGIT NLCVIGGDGS LTGADTFRSE WSDLLSDLQK SGKITAEEAT
160 170 180 190 200
KSSYLNIVGL VGSIDNDFCG TDMTIGTDSA LHRIIEIVDA ITTTAQSHQR
210 220 230 240 250
TFVLEVMGRH CGYLALVTSL SCGADWVFIP ECPPDDDWEE HLCRRLSETR
260 270 280 290 300
NRGSRLNIII VAEGAIDKNG KPITSEDIKN LVVKRLGYDT RVTVLGHVQR
310 320 330 340 350
GGTPSAFDRI LGSRMGVEAV MALLEGTPDT PACVVSLSGN QAVRLPLMEC
360 370 380 390 400
VQVTKDVTRA MDERRFDEAL KLRGRSFMNN WEVYKLLAHV RPPKSKSGSH
410 420 430 440 450
TVAVMNVGAP AAGMNAAVRS TVRIGLIQGN RMLVVHDGFE GLAKGQIEEA
460 470 480 490 500
GWSYVGGWTG QGGSKLGTKR TLPKKSFEQI SANITKFNIQ GLVIIGGFEA
510 520 530 540 550
YTGGLELMEG RKQYDELCIP FVVIPATVSN NVPGSDFSVG ADTALNTICM
560 570 580 590 600
TCDRIKQSAA GTKRRVFIIE TMGGYCGYLA TMAGLAAGAD AAYIFEDPFT
610 620 630 640 650
IRDLQVNVEH LVQKMKTTVK RGLVLRNEKC NENYTTDFIF NLYSEEGKGI
660 670 680 690 700
FDSRKNVLGH MQQGGSPTPF DRNFATKMGA KAMNWMSGKI KESYRNGRIF
710 720 730 740 750
ANSPDSGCVL GMRKRALVFQ PVTELKEQTD FEHRIPKEQW WLKLRPILKI
760 770
LAKYEIDLDT SEHAHLEHIS RKRSGEANV
Length:779
Mass (Da):85,294
Last modified:October 3, 2006 - v1
Checksum:iBBA2D207ADD079EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122655 mRNA Translation: AAI22656.1
RefSeqiNP_001068736.1, NM_001075268.1
UniGeneiBt.61411

Genome annotation databases

EnsembliENSBTAT00000000359; ENSBTAP00000000359; ENSBTAG00000000286
GeneIDi506544
KEGGibta:506544

Similar proteinsi

Entry informationi

Entry nameiPFKAM_BOVIN
AccessioniPrimary (citable) accession number: Q0IIG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 3, 2006
Last modified: May 23, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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