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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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.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 ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.UniRule annotation

Pathwayi: 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 (pgi)
  3. ATP-dependent 6-phosphofructokinase (pfkA)
  4. Probable fructose-bisphosphate aldolase (fbaA)
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)DescriptionActionsGraphical viewLength
Binding sitei11ATP; via amide nitrogenUniRule annotation1
Metal bindingi103Magnesium; catalyticUniRule annotation1
Active sitei127Proton acceptorUniRule annotation1
Binding sitei154Allosteric activator ADPUniRule annotation1
Binding sitei162Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei211Allosteric activator ADPUniRule annotation1
Binding sitei222SubstrateUniRule annotation1
Binding sitei243Substrate; shared with dimeric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi72 – 73ATPUniRule annotation2
Nucleotide bindingi102 – 105ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

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

BioCyciBSUB:BSU29190-MONOMER.
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
Synonyms:pfk
Ordered Locus Names:BSU29190
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001119361 – 319ATP-dependent 6-phosphofructokinaseAdd BLAST319

Proteomic databases

PaxDbiO34529.
PRIDEiO34529.

Interactioni

Subunit structurei

Homotetramer. Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear). Specifically interacts with RNase Y (rny, PubMed:21803996) and enolase (eno, PubMed:22198292).UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rnyO317742EBI-5250040,EBI-6415578

Protein-protein interaction databases

IntActiO34529. 4 interactors.
MINTiMINT-8366555.
STRINGi224308.Bsubs1_010100015926.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi16 – 29Combined sources14
Beta strandi33 – 37Combined sources5
Helixi42 – 46Combined sources5
Beta strandi49 – 52Combined sources4
Helixi54 – 57Combined sources4
Helixi74 – 77Combined sources4
Helixi79 – 91Combined sources13
Beta strandi96 – 101Combined sources6
Helixi105 – 114Combined sources10
Beta strandi119 – 125Combined sources7
Helixi139 – 160Combined sources22
Beta strandi163 – 168Combined sources6
Helixi175 – 184Combined sources10
Beta strandi187 – 191Combined sources5
Helixi198 – 209Combined sources12
Turni210 – 212Combined sources3
Beta strandi216 – 221Combined sources6
Turni222 – 224Combined sources3
Helixi227 – 238Combined sources12
Beta strandi242 – 246Combined sources5
Helixi248 – 252Combined sources5
Helixi258 – 275Combined sources18
Turni276 – 278Combined sources3
Beta strandi281 – 287Combined sources7
Beta strandi290 – 295Combined sources6
Helixi296 – 299Combined sources4
Beta strandi300 – 302Combined sources3
Helixi308 – 318Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A3SX-ray2.30A/B1-319[»]
ProteinModelPortaliO34529.
SMRiO34529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 25Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation5
Regioni125 – 127Substrate bindingUniRule annotation3
Regioni169 – 171Substrate bindingUniRule annotation3
Regioni185 – 187Allosteric activator ADP bindingUniRule annotation3
Regioni213 – 215Allosteric activator ADP bindingUniRule annotation3
Regioni249 – 252Substrate bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
InParanoidiO34529.
KOiK00850.
OMAiAIITICE.
PhylomeDBiO34529.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
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.

O34529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRIGVLTSG GDSPGMNAAV RAVVRKAIYH DVEVYGIYNG YAGLISGKIE
60 70 80 90 100
KLELGSVGDI IHRGGTKLYT ARCPEFKTVE GREKGIANLK KLGIEGLVVI
110 120 130 140 150
GGDGSYMGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI
160 170 180 190 200
DKIRDTATSH ERTYVIEVMG RHAGDIALWA GLAGGAESIL IPEADYDMHE
210 220 230 240 250
IIARLKRGHE RGKKHSIIIV AEGVGSGVEF GKRIEEETNL ETRVSVLGHI
260 270 280 290 300
QRGGSPSAAD RVLASRLGAY AVELLLEGKG GRCVGIQNNK LVDHDIIEIL
310
ETKHTVEQNM YQLSKELSI
Length:319
Mass (Da):34,254
Last modified:January 1, 1998 - v1
Checksum:i706CBC7F9BCFCDFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00342.1.
AL009126 Genomic DNA. Translation: CAB14879.1.
PIRiA69675.
RefSeqiNP_390797.1. NC_000964.3.
WP_003229420.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14879; CAB14879; BSU29190.
GeneIDi937376.
KEGGibsu:BSU29190.
PATRICi18977732. VBIBacSub10457_3054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00342.1.
AL009126 Genomic DNA. Translation: CAB14879.1.
PIRiA69675.
RefSeqiNP_390797.1. NC_000964.3.
WP_003229420.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A3SX-ray2.30A/B1-319[»]
ProteinModelPortaliO34529.
SMRiO34529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34529. 4 interactors.
MINTiMINT-8366555.
STRINGi224308.Bsubs1_010100015926.

Proteomic databases

PaxDbiO34529.
PRIDEiO34529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14879; CAB14879; BSU29190.
GeneIDi937376.
KEGGibsu:BSU29190.
PATRICi18977732. VBIBacSub10457_3054.

Phylogenomic databases

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
InParanoidiO34529.
KOiK00850.
OMAiAIITICE.
PhylomeDBiO34529.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciBSUB:BSU29190-MONOMER.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKA_BACSU
AccessioniPrimary (citable) accession number: O34529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.