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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

Pfkm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251ATP; via amide nitrogenUniRule annotation
Metal bindingi119 – 1191Magnesium; catalyticUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei201 – 2011Substrate; shared with dimeric partnerUniRule annotation
Binding sitei264 – 2641SubstrateUniRule annotation
Binding sitei292 – 2921Substrate; shared with dimeric partnerUniRule annotation
Binding sitei471 – 4711Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei566 – 5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei629 – 6291Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei735 – 7351Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892ATPUniRule annotation
Nucleotide bindingi118 – 1214ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. AMP binding Source: RGD
  3. ATP binding Source: RGD
  4. carbohydrate binding Source: RGD
  5. fructose-6-phosphate binding Source: RGD
  6. metal ion binding Source: UniProtKB-KW
  7. phosphofructokinase activity Source: RGD

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. cellular glucose homeostasis Source: RGD
  3. fructose 1,6-bisphosphate metabolic process Source: RGD
  4. fructose 6-phosphate metabolic process Source: RGD
  5. glycolytic process Source: RGD
  6. protein homotetramerization Source: RGD
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

SABIO-RKP47858.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi68419. Pfkm.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typePRO_0000112020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Glycosylationi530 – 5301O-linked (GlcNAc)By similarity
Modified residuei775 – 7751PhosphoserineBy similarity

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP47858.
PRIDEiP47858.

PTM databases

PhosphoSiteiP47858.

Expressioni

Gene expression databases

GenevestigatoriP47858.

Interactioni

Subunit structurei

Homo- and heterotetramers. Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).By similarity

Protein-protein interaction databases

BioGridi249268. 1 interaction.
IntActiP47858. 1 interaction.
MINTiMINT-89284.

Structurei

3D structure databases

ProteinModelPortaliP47858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 390389N-terminal catalytic PFK domain 1Add
BLAST
Regioni164 – 1663Substrate bindingUniRule annotation
Regioni208 – 2103Substrate bindingUniRule annotation
Regioni298 – 3014Substrate bindingUniRule annotation
Regioni391 – 40111Interdomain linkerAdd
BLAST
Regioni402 – 780379C-terminal regulatory PFK domain 2Add
BLAST
Regioni528 – 5325Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni573 – 5753Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni661 – 6644Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

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

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47858.
KOiK00850.
PhylomeDBiP47858.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
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]

Sequencei

Sequence statusi: Complete.

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

P47858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHEEHHEAK TLGIGKAIAV LTSGGDAQGM NATVRAVVRV GIFTGLRVFF
60 70 80 90 100
VHEGYQGLVD GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLNDLQ KDGKITAEER
160 170 180 190 200
TKSSYLNIVF 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 NTAVRLPLME
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 ISANITKYNI 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 HMQQGGNPTP FDRNFATKMG AKATNWMSGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVTELKDQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
Length:780
Mass (Da):85,560
Last modified:January 23, 2007 - v3
Checksum:iCECC3995C4F271FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331T → A in BAA21013 (Ref. 3) Curated
Sequence conflicti46 – 461L → A in BAA21013 (Ref. 3) Curated
Sequence conflicti150 – 1501R → A in BAA21013 (Ref. 3) Curated
Sequence conflicti160 – 1601F → G in BAA21013 (Ref. 3) Curated
Sequence conflicti180 – 1801S → F in BAA21013 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25651 mRNA. Translation: AAC52786.1.
D21869 mRNA. Translation: BAA21013.1.
PIRiS71429.
RefSeqiNP_113903.1. NM_031715.1.
UniGeneiRn.11004.

Genome annotation databases

GeneIDi65152.
KEGGirno:65152.
UCSCiRGD:68419. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25651 mRNA. Translation: AAC52786.1.
D21869 mRNA. Translation: BAA21013.1.
PIRiS71429.
RefSeqiNP_113903.1. NM_031715.1.
UniGeneiRn.11004.

3D structure databases

ProteinModelPortaliP47858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249268. 1 interaction.
IntActiP47858. 1 interaction.
MINTiMINT-89284.

PTM databases

PhosphoSiteiP47858.

Proteomic databases

PaxDbiP47858.
PRIDEiP47858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi65152.
KEGGirno:65152.
UCSCiRGD:68419. rat.

Organism-specific databases

CTDi5213.
RGDi68419. Pfkm.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47858.
KOiK00850.
PhylomeDBiP47858.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
SABIO-RKP47858.

Miscellaneous databases

NextBioi613989.

Gene expression databases

GenevestigatoriP47858.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
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...

Publicationsi

  1. "Characterization of expression of phosphofructokinase isoforms in isolated rat pancreatic islets and purified beta cells and cloning and expression of the rat phosphofructokinase-A isoform."
    Ma Z., Ramanadham S., Turk J., Kempe K., Hu Z., Ladenson J.
    Biochim. Biophys. Acta 1308:151-163(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Pancreatic islet.
  2. Ma Z.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 163-170 AND 494-498.
  3. Nakajima H.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-213.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiPFKAM_RAT
AccessioniPrimary (citable) accession number: P47858
Secondary accession number(s): Q63736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 123 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, Reference proteome

Documents

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

External Data

Dasty 3

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 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.