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O34529

- PFKA_BACSU

UniProt

O34529 - PFKA_BACSU

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Protein

ATP-dependent 6-phosphofructokinase

Gene
pfkA, pfk, BSU29190
Organism
Bacillus subtilis (strain 168)
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 732ATP By similarity
Nucleotide bindingi102 – 1054ATP By similarity

GO - Molecular functioni

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

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

BioCyciBSUB:BSU29190-MONOMER.
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
Ordered Locus Names:BSU29190
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU29190. [Micado]

Subcellular locationi

Cytoplasm By similarity 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_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 (1 Publication) (although rnjA and rnjB's presence is unclear). Specifically interacts with RNase Y (rny, 1 Publication) and enolase (eno, 1 Publication).

Binary interactionsi

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

Protein-protein interaction databases

IntActiO34529. 4 interactions.
MINTiMINT-8366555.
STRINGi224308.BSU29190.

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
Helixi42 – 465
Beta strandi49 – 524
Helixi54 – 574
Helixi74 – 774
Helixi79 – 9113
Beta strandi96 – 1016
Helixi105 – 11410
Beta strandi119 – 1257
Helixi139 – 16022
Beta strandi163 – 1686
Helixi175 – 18410
Beta strandi187 – 1915
Helixi198 – 20912
Turni210 – 2123
Beta strandi216 – 2216
Turni222 – 2243
Helixi227 – 23812
Beta strandi242 – 2465
Helixi248 – 2525
Helixi258 – 27518
Turni276 – 2783
Beta strandi281 – 2877
Beta strandi290 – 2956
Helixi296 – 2994
Beta strandi300 – 3023
Helixi308 – 31811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A3SX-ray2.30A/B1-319[»]
ProteinModelPortaliO34529.
SMRiO34529. Positions 1-319.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

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

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.

O34529-1 [UniParc]FASTAAdd to Basket

« Hide

MKRIGVLTSG GDSPGMNAAV RAVVRKAIYH DVEVYGIYNG YAGLISGKIE    50
KLELGSVGDI IHRGGTKLYT ARCPEFKTVE GREKGIANLK KLGIEGLVVI 100
GGDGSYMGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI 150
DKIRDTATSH ERTYVIEVMG RHAGDIALWA GLAGGAESIL IPEADYDMHE 200
IIARLKRGHE RGKKHSIIIV AEGVGSGVEF GKRIEEETNL ETRVSVLGHI 250
QRGGSPSAAD RVLASRLGAY AVELLLEGKG GRCVGIQNNK LVDHDIIEIL 300
ETKHTVEQNM YQLSKELSI 319
Length:319
Mass (Da):34,254
Last modified:January 1, 1998 - v1
Checksum:i706CBC7F9BCFCDFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008220 Genomic DNA. Translation: AAC00342.1 .
AL009126 Genomic DNA. Translation: CAB14879.1 .
PIRi A69675.
RefSeqi NP_390797.1. NC_000964.3.
WP_003229420.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A3S X-ray 2.30 A/B 1-319 [» ]
ProteinModelPortali O34529.
SMRi O34529. Positions 1-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O34529. 4 interactions.
MINTi MINT-8366555.
STRINGi 224308.BSU29190.

Proteomic databases

PaxDbi O34529.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14879 ; CAB14879 ; BSU29190 .
GeneIDi 937376.
KEGGi bsu:BSU29190.
PATRICi 18977732. VBIBacSub10457_3054.

Organism-specific databases

GenoListi BSU29190. [Micado ]

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000248870.
KOi K00850.
OMAi GFGGRCV.
OrthoDBi EOG644ZRM.
PhylomeDBi O34529.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci BSUB:BSU29190-MONOMER.

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

« 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: September 3, 2014
This is version 111 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

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