Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Mg2+UniRule annotation

Enzyme regulationi

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

Pathwayi: 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. ATP-dependent 6-phosphofructokinase (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)DescriptionActionsGraphical viewLength
Binding sitei12ATP; via amide nitrogenUniRule annotation1
Metal bindingi104Magnesium; catalyticUniRule annotation1
Active sitei129Proton acceptorUniRule annotation1
Binding sitei156Allosteric activator ADPUniRule annotation1
Binding sitei164Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei213Allosteric activator ADPUniRule annotation1
Binding sitei224SubstrateUniRule annotation1
Binding sitei245Substrate; shared with dimeric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi73 – 74ATPUniRule annotation2
Nucleotide bindingi103 – 106ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

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-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
Ordered Locus Names:HAPS_2188
OrganismiHaemophilus parasuis serovar 5 (strain SH0165)
Taxonomic identifieri557723 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000006743 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001923731 – 321ATP-dependent 6-phosphofructokinaseAdd BLAST321

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi557723.HAPS_2188.

Structurei

3D structure databases

ProteinModelPortaliB8F8G9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 26Allosteric activator ADP binding; shared with dimeric partnerUniRule annotation5
Regioni127 – 129Substrate bindingUniRule annotation3
Regioni171 – 173Substrate bindingUniRule annotation3
Regioni187 – 189Allosteric activator ADP bindingUniRule annotation3
Regioni215 – 217Allosteric activator ADP bindingUniRule annotation3
Regioni251 – 254Substrate bindingUniRule annotation4

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

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
KOiK00850.
OMAiAIITICE.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
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.

B8F8G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKKIAVLTS GGDAPGMNAA IRGVVRAGLS EGLEVYGIQD GYYGLYHDRV
60 70 80 90 100
IKLERRSVSE VINRGGTFLG SARFPEFKNP EVRAKCVETL KKYEIDALVV
110 120 130 140 150
IGGDGSYMGA KLLTEEHGIA CIGLPGTIDN DVAGTDYTIG FQTALETALE
160 170 180 190 200
AIDRLRDTST SHQRISIVEI MGRHCGDLTL SAALAGGCEY IIIPEKGFDK
210 220 230 240 250
ESLIRNIEDG FNKGKRHAII AITELMTDVH QLAREIEERF GHETRAAVLG
260 270 280 290 300
HTQRGGAPCA FDRILASRMG VYAVELLMQG YGGRCVGIQN EKLVHHDIID
310 320
AITNMRRPFK EEIFNTSRKL F
Length:321
Mass (Da):35,198
Last modified:March 3, 2009 - v1
Checksum:i37CE4D80EBE3A29A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001321 Genomic DNA. Translation: ACL33621.1.
RefSeqiWP_010786020.1. NC_011852.1.

Genome annotation databases

EnsemblBacteriaiACL33621; ACL33621; HAPS_2188.
GeneIDi7277731.
KEGGihap:HAPS_2188.
PATRICi20196734. VBIHaePar127548_2161.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001321 Genomic DNA. Translation: ACL33621.1.
RefSeqiWP_010786020.1. NC_011852.1.

3D structure databases

ProteinModelPortaliB8F8G9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi557723.HAPS_2188.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL33621; ACL33621; HAPS_2188.
GeneIDi7277731.
KEGGihap:HAPS_2188.
PATRICi20196734. VBIHaePar127548_2161.

Phylogenomic databases

eggNOGiENOG4105CTQ. Bacteria.
COG0205. LUCA.
HOGENOMiHOG000248870.
KOiK00850.
OMAiAIITICE.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

CDDicd00763. Bacterial_PFK. 1 hit.
HAMAPiMF_00339. Phosphofructokinase_I_B1. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR012003. ATP_PFK_prok-type.
IPR012828. PFKA_ATP_prok.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKA_HAEPS
AccessioniPrimary (citable) accession number: B8F8G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: November 30, 2016
This is version 51 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, Reference proteome

Documents

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

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 one 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.