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Protein

Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

Gene

pfkA

Organism
Hahella chejuensis (strain KCTC 2396)
Status
Unreviewed-Annotation score: Annotation score: 4 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

Pathway: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfkA)
  4. no protein annotated in this organism
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131Diphosphate; via amide nitrogenUniRule annotation
Metal bindingi114 – 1141Magnesium; catalyticUniRule annotation
Sitei115 – 1151Important 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
Sitei141 – 1411Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPiUniRule annotation
Active sitei144 – 1441Proton acceptorUniRule annotation
Binding sitei247 – 2471SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciHCHE349521:GHAL-5590-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:pfkAImported
Synonyms:pfpUniRule annotation
Ordered Locus Names:HCH_05798Imported
OrganismiHahella chejuensis (strain KCTC 2396)Imported
Taxonomic identifieri349521 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella
ProteomesiUP000000238 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349521.HCH_05798.

Structurei

3D structure databases

ProteinModelPortaliQ2SA75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1443Substrate bindingUniRule annotation
Regioni190 – 1923Substrate bindingUniRule annotation
Regioni297 – 3004Substrate 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.
OMAiITIVEIM.
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.

Q2SA75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVKNAFYAQ SGGVTSVINA SACGVLETAR AHSDKIGKVY AGHNGIIGAL
60 70 80 90 100
REELIDTSLE SDADIAALKH TPGGAFGSCR YKLKDIKTHK AEYERLIEVF
110 120 130 140 150
KAHNIGYFFY NGGNDSSDTA YKVSQISEQL GYPITSIGIP KTVDNDLPIT
160 170 180 190 200
DCCPGFGSVA KYISTSIMEA SLDIQSMCES STKIFVMEVM GRHAGWIAAA
210 220 230 240 250
AGLAQREEGG APQIILFPET PFDKASFLRR VDEVVKRDGF CAIVVSEGAQ
260 270 280 290 300
YADGRFLSDA GVTDAFGHTQ LGGVAPFIAN MIKSELGYKY HWAVADYLQR
310 320 330 340 350
SARHISSATD LDQAYAVGKA AVDLALAGKN AVMPVIVREQ DSPYKWSVGE
360 370 380 390 400
APLAKIANVE KKMPKEFITE DGFGITEAAR RYLQPLIQGE SYPPYKNGVP
410 420
DYVKLKNQLV AKKLAHSFNV
Length:420
Mass (Da):45,476
Last modified:January 24, 2006 - v1
Checksum:i9260071CFD1B0EF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000155 Genomic DNA. Translation: ABC32449.1.
RefSeqiWP_011399508.1. NC_007645.1.
YP_436874.1. NC_007645.1.

Genome annotation databases

EnsemblBacteriaiABC32449; ABC32449; HCH_05798.
KEGGihch:HCH_05798.
PATRICi22091826. VBIHahChe29232_5258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000155 Genomic DNA. Translation: ABC32449.1.
RefSeqiWP_011399508.1. NC_007645.1.
YP_436874.1. NC_007645.1.

3D structure databases

ProteinModelPortaliQ2SA75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349521.HCH_05798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC32449; ABC32449; HCH_05798.
KEGGihch:HCH_05798.
PATRICi22091826. VBIHahChe29232_5258.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000007357.
KOiK00850.
OMAiITIVEIM.
OrthoDBiEOG6PP9HS.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciHCHE349521:GHAL-5590-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: KCTC 2396Imported.

Entry informationi

Entry nameiQ2SA75_HAHCH
AccessioniPrimary (citable) accession number: Q2SA75
Entry historyi
Integrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: May 27, 2015
This is version 67 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.