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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

Pathway:iglycolysis

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)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 sitei211 – 2111Allosteric activator ADPUniRule 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

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
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU29190. [Micado]

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319ATP-dependent 6-phosphofructokinasePRO_0000111936Add
BLAST

Proteomic databases

PaxDbiO34529.

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 interactions.
MINTiMINT-8366555.
STRINGi224308.Bsubs1_010100015926.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi16 – 2914Combined sources
Beta strandi33 – 375Combined sources
Helixi42 – 465Combined sources
Beta strandi49 – 524Combined sources
Helixi54 – 574Combined sources
Helixi74 – 774Combined sources
Helixi79 – 9113Combined sources
Beta strandi96 – 1016Combined sources
Helixi105 – 11410Combined sources
Beta strandi119 – 1257Combined sources
Helixi139 – 16022Combined sources
Beta strandi163 – 1686Combined sources
Helixi175 – 18410Combined sources
Beta strandi187 – 1915Combined sources
Helixi198 – 20912Combined sources
Turni210 – 2123Combined sources
Beta strandi216 – 2216Combined sources
Turni222 – 2243Combined sources
Helixi227 – 23812Combined sources
Beta strandi242 – 2465Combined sources
Helixi248 – 2525Combined sources
Helixi258 – 27518Combined sources
Turni276 – 2783Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi290 – 2956Combined sources
Helixi296 – 2994Combined sources
Beta strandi300 – 3023Combined sources
Helixi308 – 31811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A3SX-ray2.30A/B1-319[»]
ProteinModelPortaliO34529.
SMRiO34529. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

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

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000248870.
InParanoidiO34529.
KOiK00850.
OMAiGFGGRCV.
OrthoDBiEOG644ZRM.
PhylomeDBiO34529.

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
4A3SX-ray2.30A/B1-319[»]
ProteinModelPortaliO34529.
SMRiO34529. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiO34529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU29190. [Micado]

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000248870.
InParanoidiO34529.
KOiK00850.
OMAiGFGGRCV.
OrthoDBiEOG644ZRM.
PhylomeDBiO34529.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciBSUB:BSU29190-MONOMER.

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing."
    Commichau F.M., Rothe F.M., Herzberg C., Wagner E., Hellwig D., Lehnik-Habrink M., Hammer E., Volker U., Stulke J.
    Mol. Cell. Proteomics 8:1350-1360(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: 168.
  4. "RNase Y in Bacillus subtilis: a natively disordered protein that is the functional equivalent of RNase E from Escherichia coli."
    Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S., Rodrigues C., Herzberg C., Commichau F.M., Lewis R.J., Stulke J.
    J. Bacteriol. 193:5431-5441(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNY, SUBUNIT.
    Strain: 168.
  5. "Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome."
    Newman J.A., Hewitt L., Rodrigues C., Solovyova A.S., Harwood C.R., Lewis R.J.
    J. Mol. Biol. 416:121-136(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH ENO, SUBUNIT.
    Strain: 168.

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: July 22, 2015
This is version 119 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

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.