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P80019

- PFKA_LACDE

UniProt

P80019 - PFKA_LACDE

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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Lactobacillus delbrueckii subsp. bulgaricus
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 PublicationUniRule 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 and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. The binding affinities for these effectors are decreased however, and therefore the allosteric effect becomes apparent only at high effector concentrations.2 PublicationsUniRule annotation

Kineticsi

  1. KM=0.2 mM for ATP (at pH 8.2)1 Publication
  2. KM=0.07 mM for ATP (at pH 6.0)1 Publication
  3. KM=0.3 mM for fructose 6-phosphate (at pH 6.0 and 8.2)1 Publication

Vmax=90 µmol/min/mg enzyme (at pH 8.2)1 Publication

pH dependencei

Optimum pH is 8.2.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111ATP; via amide nitrogenUniRule annotation
Metal bindingi103 – 1031Magnesium; catalyticUniRule annotation
Active sitei127 – 1271Proton acceptorUniRule annotation
Binding sitei154 – 1541Allosteric activator ADPUniRule annotation
Binding sitei162 – 1621Substrate; shared with dimeric partnerUniRule annotation
Binding sitei222 – 2221SubstrateUniRule annotation
Binding sitei243 – 2431Substrate; shared with dimeric partnerUniRule annotation

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-RKP80019.
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:pfkAUniRule annotation
OrganismiLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifieri1585 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319ATP-dependent 6-phosphofructokinasePRO_0000111957Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 PublicationUniRule annotation

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi16 – 2813Combined sources
Turni29 – 313Combined sources
Beta strandi33 – 375Combined sources
Helixi40 – 467Combined sources
Beta strandi49 – 513Combined sources
Helixi54 – 574Combined sources
Helixi74 – 763Combined sources
Helixi79 – 9113Combined sources
Beta strandi96 – 1016Combined sources
Helixi103 – 11412Combined sources
Beta strandi119 – 1257Combined sources
Helixi139 – 15921Combined sources
Beta strandi163 – 1686Combined sources
Helixi175 – 1839Combined sources
Beta strandi187 – 1904Combined sources
Helixi198 – 21013Combined sources
Beta strandi216 – 2216Combined sources
Turni222 – 2243Combined sources
Helixi227 – 23610Combined sources
Beta strandi242 – 2465Combined sources
Helixi248 – 2525Combined sources
Helixi258 – 27619Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi290 – 2956Combined sources
Helixi296 – 2994Combined sources
Helixi309 – 3179Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXXX-ray1.85A1-319[»]
ProteinModelPortaliP80019.
SMRiP80019. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80019.

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

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.UniRule annotation

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
InterProiIPR012003. ATP_PFK_prok-type.
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.

P80019-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRIGILTSG GDAPGMNAAV RAVTRVAIAN GLEVFGIRYG FAGLVAGDIF
60 70 80 90 100
PLESEDVAHL INVSGTFLYS ARYPEFAEEE GQLAGIEQLK KHGIDAVVVI
110 120 130 140 150
GGDGSYHGAL QLTRHGFNSI GLPGTIDNDI PYTDATIGYD TACMTAMDAI
160 170 180 190 200
DKIRDTASSH HRVFIVNVMG RNCGDIAMRV GVACGADAIV IPERPYDVEE
210 220 230 240 250
IANRLKQAQE SGKDHGLVVV AEGVMTADQF MAELKKYGDF DVRANVLGHM
260 270 280 290 300
QRGGTPTVSD RVLASKLGSE AVHLLLEGKG GLAVGIENGK VTSHDILDLF
310
DESHRGDYDL LKLNADLSR
Length:319
Mass (Da):34,009
Last modified:June 1, 1994 - v2
Checksum:i555C5FE1D522BC9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50526.1.
PIRiA48663. S35928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71403 Genomic DNA. Translation: CAA50526.1 .
PIRi A48663. S35928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZXX X-ray 1.85 A 1-319 [» ]
ProteinModelPortali P80019.
SMRi P80019. Positions 1-319.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P80019.

Miscellaneous databases

EvolutionaryTracei P80019.

Family and domain databases

HAMAPi MF_00339. Phosphofructokinase_I_B1.
InterProi IPR012003. ATP_PFK_prok-type.
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. "Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 175:5344-5349(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Purification and properties of the phosphofructokinase from Lactobacillus bulgaricus. A non-allosteric analog of the enzyme from Escherichia coli."
    le Bras G., Deville-Bonne D., Garel J.R.
    Eur. J. Biochem. 198:683-687(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-38, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    Strain: B107.
  3. "Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus."
    Paricharttanakul N.M., Ye S., Menefee A.L., Javid-Majd F., Sacchettini J.C., Reinhart G.D.
    Biochemistry 44:15280-15286(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), ENZYME REGULATION.
    Strain: B107.

Entry informationi

Entry nameiPFKA_LACDE
AccessioniPrimary (citable) accession number: P80019
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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