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Q9L1L8

- PFKA2_STRCO

UniProt

Q9L1L8 - PFKA2_STRCO

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Protein

ATP-dependent 6-phosphofructokinase 2

Gene

pfkA2

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Mg2+1 PublicationUniRule annotation

Enzyme regulationi

Allosterically inhibited by phosphoenolpyruvate.1 Publication

Kineticsi

  1. KM=0.4 mM for ATP1 Publication

Vmax=165 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5-8.1 Publication

Temperature dependencei

Optimum temperature is 30-50 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101ATP; via amide nitrogenUniRule annotation
Metal bindingi103 – 1031Magnesium; catalyticUniRule annotation
Sitei104 – 1041Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation
Active sitei127 – 1271Proton acceptorUniRule annotation
Binding sitei162 – 1621Substrate; shared with dimeric partnerUniRule annotation
Binding sitei222 – 2221SubstrateUniRule annotation
Binding sitei266 – 2661Substrate; 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-EC
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
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

UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 2UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 2UniRule annotation
Short name:
Phosphofructokinase 2UniRule annotation
Alternative name(s):
Phosphohexokinase 2UniRule annotation
Gene namesi
Name:pfkA2UniRule annotation
Synonyms:pfk2
Ordered Locus Names:SCO5426
ORF Names:SC6A11.02
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Accumulates glucose 6-phosphate and fructose 6-phosphate. Has an increased carbon flux through the pentose phosphate pathway, resulting in a higher production of the pigmented antibiotics actinorhodin and undecylprodigiosin.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341ATP-dependent 6-phosphofructokinase 2PRO_0000111987Add
BLAST

Proteomic databases

PRIDEiQ9L1L8.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO5426.

Structurei

3D structure databases

ProteinModelPortaliQ9L1L8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 1273Substrate bindingUniRule annotation
Regioni169 – 1713Substrate bindingUniRule annotation
Regioni272 – 2754Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000248869.
InParanoidiQ9L1L8.
KOiK00850.
OMAiRGDFGRM.
OrthoDBiEOG644ZRM.
PhylomeDBiQ9L1L8.

Family and domain databases

HAMAPiMF_01976. Phosphofructokinase_III.
InterProiIPR012003. ATP_PFK_prok-type.
IPR012829. PFK.
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.
TIGRFAMsiTIGR02483. PFK_mixed. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9L1L8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRIGVLTAGG DCPGLNAVIR SVVHRAVDNY GDEVIGFEDG YAGLLDGRYR
60 70 80 90 100
ALDLNAVSGI LARGGTILGS SRLERDRLRE ACENAGDMIQ NFGIDALIPI
110 120 130 140 150
GGEGTLTAAR MLSDAGLPVV GVPKTIDNDI SSTDRTFGFD TAVGVATEAM
160 170 180 190 200
DRLKTTAESH QRVMVVEVMG RHAGWIALES GMAAGAHGIC LPERPFDPAD
210 220 230 240 250
LVKMVEERFS RGKKFAVVCV AEGAHPAEGS MDYGKGAIDK FGHERFQGIG
260 270 280 290 300
TALAFELERR LGKEAKPVIL GHVQRGGVPT AYDRVLATRF GWHAVEAAHR
310 320 330 340
GDFGRMTALR GTDVVMVPLA EAVTELKTVP KDRMDEAESV F
Length:341
Mass (Da):36,434
Last modified:October 1, 2000 - v1
Checksum:i6C0B09B76FE90BBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939123 Genomic DNA. Translation: CAB72402.1.
RefSeqiNP_629564.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB72402; CAB72402; CAB72402.
GeneIDi1100866.
KEGGisco:SCO5426.
PATRICi23740702. VBIStrCoe124346_5507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939123 Genomic DNA. Translation: CAB72402.1 .
RefSeqi NP_629564.1. NC_003888.3.

3D structure databases

ProteinModelPortali Q9L1L8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO5426.

Proteomic databases

PRIDEi Q9L1L8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB72402 ; CAB72402 ; CAB72402 .
GeneIDi 1100866.
KEGGi sco:SCO5426.
PATRICi 23740702. VBIStrCoe124346_5507.

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000248869.
InParanoidi Q9L1L8.
KOi K00850.
OMAi RGDFGRM.
OrthoDBi EOG644ZRM.
PhylomeDBi Q9L1L8.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .

Family and domain databases

HAMAPi MF_01976. Phosphofructokinase_III.
InterProi IPR012003. ATP_PFK_prok-type.
IPR012829. PFK.
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 TIGR02483. PFK_mixed. 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 BAA-471 / A3(2) / M145.
  2. "Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)."
    Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L.
    Appl. Environ. Microbiol. 63:956-961(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 1-28, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION.
    Strain: A3(2) / 1109.
  3. "Antibiotic overproduction in Streptomyces coelicolor A3(2) mediated by phosphofructokinase deletion."
    Borodina I., Siebring J., Zhang J., Smith C.P., van Keulen G., Dijkhuizen L., Nielsen J.
    J. Biol. Chem. 283:25186-25199(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPFKA2_STRCO
AccessioniPrimary (citable) accession number: Q9L1L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The nucleotide sequence reported in PubMed:9055413 was not that of the characterized enzyme. Inspection of the original N-terminal sequence showed that the characterized enzyme was pfkA2 (SCO5426) and not pfkA1 (SCO2119), another isozyme in S.coelicolor (PubMed:18606812).1 Publication

Keywords - Technical termi

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