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P00512

- PFKA_GEOSE

UniProt

P00512 - PFKA_GEOSE

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Protein

ATP-dependent 6-phosphofructokinase

Gene
pfkA, pfk
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation

Kineticsi

  1. KM=0.07 mM for ATP1 Publication
  2. KM=0.033 mM for fructose 6-phosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111ATP; via amide nitrogen
Binding sitei59 – 591Allosteric activator ADP; shared with dimeric partner
Metal bindingi103 – 1031Magnesium; catalytic By similarity
Active sitei127 – 1271Proton acceptor
Binding sitei154 – 1541Allosteric activator ADP
Binding sitei162 – 1621Substrate; shared with dimeric partner
Binding sitei211 – 2111Allosteric activator ADP
Binding sitei222 – 2221Substrate
Binding sitei243 – 2431Substrate; shared with dimeric partner

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 732ATPUniRule annotation
Nucleotide bindingi102 – 1054ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-HAMAP
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-RKP00512.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
Phosphofructokinase
Alternative name(s):
Phosphohexokinase
Gene namesi
Name:pfkA
Synonyms:pfk
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319ATP-dependent 6-phosphofructokinaseUniRule annotationPRO_0000111935Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Helixi16 – 2914
Beta strandi33 – 375
Helixi40 – 467
Beta strandi49 – 524
Helixi54 – 574
Helixi74 – 774
Helixi81 – 9111
Beta strandi97 – 1026
Helixi103 – 11412
Beta strandi119 – 1279
Helixi139 – 15315
Beta strandi159 – 16810
Helixi175 – 1839
Beta strandi187 – 1904
Helixi198 – 21013
Beta strandi216 – 2216
Turni222 – 2243
Helixi227 – 23812
Beta strandi241 – 2466
Helixi248 – 2525
Helixi258 – 27720
Beta strandi281 – 2877
Beta strandi290 – 2956
Helixi296 – 3005
Helixi308 – 31710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MTOX-ray3.20A/B/C/D/E/F/G/H1-319[»]
3PFKX-ray2.40A1-319[»]
3U39X-ray2.79A/B/C/D1-319[»]
4I36X-ray2.30A/B/C/D1-319[»]
4I4IX-ray2.49A/B/C/D1-319[»]
4I7EX-ray2.00A/B/C/D1-319[»]
4PFKX-ray2.40A1-319[»]
6PFKX-ray2.60A/B/C/D1-319[»]
ProteinModelPortaliP00512.
SMRiP00512. Positions 1-319.

Miscellaneous databases

EvolutionaryTraceiP00512.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation
Regioni125 – 1273Substrate bindingUniRule annotation
Regioni169 – 1713Substrate bindingUniRule annotation
Regioni185 – 1873Allosteric activator ADP bindingUniRule annotation
Regioni213 – 2153Allosteric activator ADP bindingUniRule annotation
Regioni249 – 2524Substrate bindingUniRule annotation

Sequence similaritiesi

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
InterProiIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00512-1 [UniParc]FASTAAdd to Basket

« Hide

MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK    50
KLEVGDVGDI IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI 100
GGDGSYQGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI 150
DKIRDTATSH ERTYVIEVMG RHAGDIALWS GLAGGAETIL IPEADYDMND 200
VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF ETRVTVLGHV 250
QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL 300
ANKHTIDQRM YALSKELSI 319
Length:319
Mass (Da):34,119
Last modified:July 1, 1989 - v2
Checksum:iEE968D39BA30712B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121D → N AA sequence 1 Publication
Sequence conflicti35 – 373Missing AA sequence 1 Publication
Sequence conflicti43 – 431G → V AA sequence 1 Publication
Sequence conflicti82 – 821Q → E AA sequence 1 Publication
Sequence conflicti95 – 951E → Q AA sequence 1 Publication
Sequence conflicti225 – 2251G → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15643 Genomic DNA. Translation: AAA22656.1.
D13095 Genomic DNA. Translation: BAA02405.1.
PIRiA27474. KIBSFF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15643 Genomic DNA. Translation: AAA22656.1 .
D13095 Genomic DNA. Translation: BAA02405.1 .
PIRi A27474. KIBSFF.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MTO X-ray 3.20 A/B/C/D/E/F/G/H 1-319 [» ]
3PFK X-ray 2.40 A 1-319 [» ]
3U39 X-ray 2.79 A/B/C/D 1-319 [» ]
4I36 X-ray 2.30 A/B/C/D 1-319 [» ]
4I4I X-ray 2.49 A/B/C/D 1-319 [» ]
4I7E X-ray 2.00 A/B/C/D 1-319 [» ]
4PFK X-ray 2.40 A 1-319 [» ]
6PFK X-ray 2.60 A/B/C/D 1-319 [» ]
ProteinModelPortali P00512.
SMRi P00512. Positions 1-319.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P00512.

Miscellaneous databases

EvolutionaryTracei P00512.

Family and domain databases

HAMAPi MF_00339. Phosphofructokinase_I_B1.
InterProi IPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 1 hit.
TIGRFAMsi TIGR02482. PFKA_ATP. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene."
    French B.A., Chang S.H.
    Gene 54:65-71(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus."
    Kolb E., Hudson P.J., Harris J.I.
    Eur. J. Biochem. 108:587-597(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  3. "Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."
    Sakai H., Ohta T.
    Eur. J. Biochem. 211:851-859(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319.
  4. "Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme."
    Byrnes M., Zhu X., Younathan E.S., Chang S.H.
    Biochemistry 33:3424-3431(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "Structure and control of phosphofructokinase from Bacillus stearothermophilus."
    Evans P.R., Hudson P.J.
    Nature 279:500-504(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP AND FRUCTOSE-6-PHOSPHATE.
  7. "Structural basis of the allosteric behaviour of phosphofructokinase."
    Schirmer T., Evans P.R.
    Nature 343:140-145(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.
  8. "Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus."
    Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D.
    Biochemistry 41:12967-12974(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
  9. "Structure of the apo form of Bacillus stearothermophilus phosphofructokinase."
    Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
    Biochemistry 51:769-775(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS).
  10. "Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase."
    Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.
    Biochemistry 52:5421-5429(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVIC ACID.

Entry informationi

Entry nameiPFKA_GEOSE
AccessioniPrimary (citable) accession number: P00512
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP.
The phosphate group of phosphoenolpyruvate appears to bind in the same place as the beta-phosphate group of ADP.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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