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Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Medicago truncatula (Barrel medic) (Medicago tribuloides)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 AMP.UniRule annotation

Pathway: 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, Glucose-6-phosphate isomerase (MTR_6g009330), Glucose-6-phosphate isomerase (MTR_5g065880)
  3. ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP-BETA), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK)
  4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (MTR_1g109200), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (MTR_1g061050), Fructose-bisphosphate aldolase (MTR_7g103920), Fructose-bisphosphate aldolase (MTR_4g057670), Fructose-bisphosphate aldolase (MTR_4g071860), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (MTR_5g069050), Fructose-bisphosphate aldolase (MTR_4g071880), Fructose-bisphosphate aldolase (MTR_5g096670), Fructose-bisphosphate aldolase (MTR_5g069055), Fructose-bisphosphate aldolase
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981ATP; via amide nitrogenUniRule annotation
Metal bindingi187 – 1871Magnesium; catalyticUniRule annotation
Sitei188 – 1881Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation
Active sitei217 – 2171Proton acceptorUniRule annotation
Binding sitei316 – 3161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1622ATPUniRule annotation
Nucleotide bindingi186 – 1894ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PhosphofructokinaseUniRule annotation
Alternative name(s):
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKUniRule annotation
Ordered Locus Names:MTR_6g090130Imported
OrganismiMedicago truncatula (Barrel medic) (Medicago tribuloides)Imported
Taxonomic identifieri3880 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago
ProteomesiUP000002051 Componenti: Chromosome 6

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 2173Substrate bindingUniRule annotation
Regioni260 – 2623Substrate bindingUniRule annotation
Regioni373 – 3764Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade "X" sub-subfamily.UniRule annotation

Phylogenomic databases

KOiK00850.
OMAiNERATED.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_TP0108.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

G7KHY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLTEPKVVT GPAGYVLEDV PHLSDYIPDL PTYPNPLQDN PAYSVVKQYF
60 70 80 90 100
VHVDDTVPQK VVVHKDSPRG VHFRRAGPRQ KVYFESDEIQ AAIVTCGGLC
110 120 130 140 150
PGLNTVIREL VCSLHHMYGV TRVLGIEGGY RGFYARNTIT LTPSSVNNIH
160 170 180 190 200
KRGGTILGTS RGGHDTNKIV DSIQDRGINQ VYIIGGDGTQ RGASVIFEEV
210 220 230 240 250
RRRGLKCAVV GIPKTIDNDI PIIDKSFGFD TAVEEAQRAI NAAHVEAESF
260 270 280 290 300
ENGIGVVKLM GRYSGFIAMY ATLASRDVDC CLIPESPFYL EGPGGLYEYI
310 320 330 340 350
DRRLKENGHM VIVIAEGAGQ ELLTESLQSG KKQDASGNKL LQDVGLWISQ
360 370 380 390 400
SIKDHFAREK TLPITLKYID PTYMIRAVPS NASDNVYCTL LAQSAVHGAM
410 420 430 440 450
AGYTGYTSGL VNGRQTYIPF YRITERQNNV VITDRMWARL LSSTNQPSFM
460 470 480 490 500
EVKVSDEDTK GENSLDELPD GHCSEDTSVD EITHNLGCLA PLAVPVLRTG

GISGV
Length:505
Mass (Da):55,211
Last modified:January 25, 2012 - v1
Checksum:iA8EDBD79C00E34E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM001222 Genomic DNA. Translation: AES76981.1.
RefSeqiXP_003620763.1. XM_003620715.1.
UniGeneiMtr.5379.

Genome annotation databases

EnsemblPlantsiAES76981; AES76981; MTR_6g090130.
GeneIDi11438579.
KEGGimtr:MTR_6g090130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM001222 Genomic DNA. Translation: AES76981.1.
RefSeqiXP_003620763.1. XM_003620715.1.
UniGeneiMtr.5379.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAES76981; AES76981; MTR_6g090130.
GeneIDi11438579.
KEGGimtr:MTR_6g090130.

Phylogenomic databases

KOiK00850.
OMAiNERATED.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_TP0108.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Medicago genome provides insight into the evolution of rhizobial symbioses."
    Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V.
    , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
    Nature 480:520-524(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A17Imported and cv. Jemalong A17Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A17.
  3. EnsemblPlants
    Submitted (APR-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: cv. Jemalong A17Imported.

Entry informationi

Entry nameiG7KHY6_MEDTR
AccessioniPrimary (citable) accession number: G7KHY6
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: June 24, 2015
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Allosteric enzymeUniRule annotation, Complete proteome, Reference proteomeImported

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.