Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O34529

- PFKA_BACSU

UniProt

O34529 - PFKA_BACSU

Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Magnesium.UniRule annotation

    Enzyme regulationi

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

    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 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

    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

    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: Chromosome

    Organism-specific databases

    GenoListiBSU29190. [Micado]

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    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).3 PublicationsUniRule annotation

    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.
    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.
    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

    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: October 1, 2014
    This is version 112 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