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P47858

- PFKAM_RAT

UniProt

P47858 - PFKAM_RAT

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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

Pfkm

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Magnesium.

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-KW
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. 1 PublicationCurated
Sequence conflicti46 – 461L → A in BAA21013. 1 PublicationCurated
Sequence conflicti150 – 1501R → A in BAA21013. 1 PublicationCurated
Sequence conflicti160 – 1601F → G in BAA21013. 1 PublicationCurated
Sequence conflicti180 – 1801S → F in BAA21013. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U25651 mRNA. Translation: AAC52786.1 .
D21869 mRNA. Translation: BAA21013.1 .
PIRi S71429.
RefSeqi NP_113903.1. NM_031715.1.
UniGenei Rn.11004.

3D structure databases

ProteinModelPortali P47858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249268. 1 interaction.
IntActi P47858. 1 interaction.
MINTi MINT-89284.

PTM databases

PhosphoSitei P47858.

Proteomic databases

PaxDbi P47858.
PRIDEi P47858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65152.
KEGGi rno:65152.
UCSCi RGD:68419. rat.

Organism-specific databases

CTDi 5213.
RGDi 68419. Pfkm.

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi P47858.
KOi K00850.
PhylomeDBi P47858.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P47858.

Miscellaneous databases

NextBioi 613989.

Gene expression databases

Genevestigatori P47858.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 120 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