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Q9WY52

- PFKA_THEMA

UniProt

Q9WY52 - PFKA_THEMA

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Protein

ATP-dependent 6-phosphofructokinase

Gene
pfkA, TM_0209
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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.2 Publications

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.2 Publications

Cofactori

Magnesium. Can partially be replaced by manganese and iron.1 Publication

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. Strongly inhibited by diphosphate, triphosphate and polyphosphate.1 Publication

Kineticsi

  1. KM=0.2 mM for ATP (at 75 degrees Celsius)2 Publications
  2. KM=7.6 mM for fructose 1,6-bisphosphate (at 75 degrees Celsius)
  3. KM=1.4 mM for ADP (at 75 degrees Celsius)

Vmax=360 µmol/min/mg enzyme for the forward reaction (at 75 degrees Celsius)

Vmax=432 µmol/min/mg enzyme for the forward reaction (at 50 degrees Celsius)

Vmax=13 µmol/min/mg enzyme for the reverse reaction (at 75 degrees Celsius)

pH dependencei

Optimum pH is 6.7.

Temperature dependencei

Optimum temperature is 93 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111ATP; via amide nitrogen By similarity
Metal bindingi103 – 1031Magnesium; catalytic By similarity
Active sitei128 – 1281Proton acceptor By similarity
Binding sitei155 – 1551Allosteric activator ADP By similarity
Binding sitei163 – 1631Substrate; shared with dimeric partner By similarity
Binding sitei212 – 2121Allosteric activator ADP By similarity
Binding sitei223 – 2231Substrate By similarity
Binding sitei244 – 2441Substrate; 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

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

BioCyciMetaCyc:MONOMER-363.
SABIO-RKQ9WY52.
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
Ordered Locus Names:TM_0209
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

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_0000112000Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi243274.TM0209.

Structurei

3D structure databases

ProteinModelPortaliQ9WY52.
SMRiQ9WY52. Positions 1-319.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Regioni126 – 1283Substrate binding By similarity
Regioni170 – 1723Substrate binding By similarity
Regioni186 – 1883Allosteric activator ADP binding By similarity
Regioni214 – 2163Allosteric activator ADP binding By similarity
Regioni250 – 2534Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0205.
KOiK00850.
OMAiGFGGRCV.
OrthoDBiEOG644ZRM.

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.

Q9WY52-1 [UniParc]FASTAAdd to Basket

« Hide

MKKIAVLTSG GDAPGMNAAV RAVVRYGVRQ GLEVIGVRRG YSGLIDGDFV    50
KLEYKDVAGI TEKGGTILRT SRCEEFKTEE GRELAAKQIK KHGIEGLVVI 100
GGEGSLTGAH LLYEEHKIPV VGIPATIDND IGLTDMCIGV DTCLNTVMDA 150
VQKLKDTASS HERAFIVEVM GRHSGYIALM AGLVTGAEAI IVPEIPVDYS 200
QLADRILEER RRGKINSIII VAEGAASAYT VARHLEYRIG YETRITILGH 250
VQRGGSPTAF DRRLALSMGV EAVDALLDGE VDVMIALQGN KFVRVPIMEA 300
LSTKKTIDKK LYEIAHMLS 319
Length:319
Mass (Da):34,487
Last modified:November 1, 1999 - v1
Checksum:i3809E971288D12B8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21K → R AA sequence 1 Publication
Sequence conflicti14 – 174PGMN → GPM AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35301.1.
PIRiC72406.
RefSeqiNP_228024.1. NC_000853.1.
YP_007976558.1. NC_021214.1.
YP_008990817.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35301; AAD35301; TM_0209.
GeneIDi897081.
KEGGitma:TM0209.
tmi:THEMA_03680.
tmm:Tmari_0207.
PATRICi23935290. VBITheMar51294_0211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35301.1 .
PIRi C72406.
RefSeqi NP_228024.1. NC_000853.1.
YP_007976558.1. NC_021214.1.
YP_008990817.1. NC_023151.1.

3D structure databases

ProteinModelPortali Q9WY52.
SMRi Q9WY52. Positions 1-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0209.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35301 ; AAD35301 ; TM_0209 .
GeneIDi 897081.
KEGGi tma:TM0209.
tmi:THEMA_03680.
tmm:Tmari_0207.
PATRICi 23935290. VBITheMar51294_0211.

Phylogenomic databases

eggNOGi COG0205.
KOi K00850.
OMAi GFGGRCV.
OrthoDBi EOG644ZRM.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci MetaCyc:MONOMER-363.
SABIO-RK Q9WY52.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "ATP-dependent 6-phosphofructokinase from the hyperthermophilic bacterium Thermotoga maritima: characterization of an extremely thermophilic, allosterically regulated enzyme."
    Hansen T., Musfeldt M., Schonheit P.
    Arch. Microbiol. 177:401-409(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-39, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes."
    Ding Y.R., Ronimus R.S., Morgan H.W.
    J. Bacteriol. 183:791-794(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiPFKA_THEMA
AccessioniPrimary (citable) accession number: Q9WY52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 97 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

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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