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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfp

Organism
Magnetococcus sp. (strain MC-1)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Non-allosteric.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131Diphosphate; via amide nitrogenUniRule annotation
Metal bindingi108 – 1081Magnesium; catalyticUniRule annotation
Sitei109 – 1091Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATPUniRule annotation
Sitei135 – 1351Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei138 – 1381Proton acceptorUniRule annotation
Binding sitei237 – 2371SubstrateUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-EC

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciMSP156889:GH36-1941-MONOMER.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrophosphate--fructose 6-phosphate 1-phosphotransferaseUniRule annotation (EC:2.7.1.90UniRule annotation)
Alternative name(s):
6-phosphofructokinase, pyrophosphate dependentUniRule annotation
PPi-dependent phosphofructokinaseUniRule annotation
Pyrophosphate-dependent 6-phosphofructose-1-kinaseUniRule annotation
Gene namesi
Name:pfpUniRule annotation
Ordered Locus Names:Mmc1_1917Imported
OrganismiMagnetococcus sp. (strain MC-1)Imported
Taxonomic identifieri156889 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
ProteomesiUP000002586 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi156889.Mmc1_1917.

Structurei

3D structure databases

ProteinModelPortaliA0L8Y2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 1383Substrate bindingUniRule annotation
Regioni180 – 1823Substrate bindingUniRule annotation
Regioni295 – 2984Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade "B2" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000007357.
KOiK00850.
OMAiCGVIETA.
OrthoDBiEOG6PP9HS.

Family and domain databases

HAMAPiMF_01978. Phosphofructokinase_II_B2.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011404. PPi-PFK_XF0274.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036483. PFK_XF0274. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

A0L8Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSGKVLIAQ GGGPTAVINQ SLVGAVLEAQ RYAQVDRIYG AVHGVRGIVD
60 70 80 90 100
ENFMDLSMET AGNLERVAAM PSSALGSTRD KPDRAYCAEM FKVLKAHDIR
110 120 130 140 150
SFFYCGGNDS SDTVRIVKEF ADEANYEFTA MHIPKTIDND LMANDHTPGF
160 170 180 190 200
PSAAKFVACA FAGVNMDNRA LPGVYVGVVM GRHAGFLTGA AAMARVFADD
210 220 230 240 250
GPHLIYVPER TFDMNTFLAD VKSTYDKYGR CIVAVSEGVH DAEGTPIVTK
260 270 280 290 300
LQENVERDAH GNVQLSGTGA LADLLCDEIK AKLGIKRVRG DTFGYLQRSF
310 320 330 340 350
LGIVSEVDAR EAREVGQKAV QEALRHNASG TITIKRVGNY ASAYELANVK
360 370 380 390 400
EVAALTKVMA DNFITTASND VTADFIHYLR PLLGSNPLEH AARLMAPMVE

KILHK
Length:405
Mass (Da):43,825
Last modified:December 12, 2006 - v1
Checksum:i72304F5D34BBD1D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK44425.1.
RefSeqiYP_865831.1. NC_008576.1.

Genome annotation databases

EnsemblBacteriaiABK44425; ABK44425; Mmc1_1917.
KEGGimgm:Mmc1_1917.
PATRICi22430445. VBIMagSp23654_1972.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK44425.1.
RefSeqiYP_865831.1. NC_008576.1.

3D structure databases

ProteinModelPortaliA0L8Y2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi156889.Mmc1_1917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK44425; ABK44425; Mmc1_1917.
KEGGimgm:Mmc1_1917.
PATRICi22430445. VBIMagSp23654_1972.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000007357.
KOiK00850.
OMAiCGVIETA.
OrthoDBiEOG6PP9HS.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciMSP156889:GH36-1941-MONOMER.

Family and domain databases

HAMAPiMF_01978. Phosphofructokinase_II_B2.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR011404. PPi-PFK_XF0274.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF036483. PFK_XF0274. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC-1Imported.

Entry informationi

Entry nameiA0L8Y2_MAGSM
AccessioniPrimary (citable) accession number: A0L8Y2
Entry historyi
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: April 29, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.