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Q9KNP2 (PFKA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:VC_2689
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.

Sequence caution

The sequence AAF95830.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000112005

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP By similarity
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region186 – 1883Allosteric activator ADP binding By similarity
Region214 – 2163Allosteric activator ADP binding By similarity
Region250 – 2534Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site121ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2441Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KNP2 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 552D3665CB63EB76

FASTA32034,670
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRTALG AGLEVFGIYD GYQGLYEDRI KQLDRSSVSD 

        70         80         90        100        110        120 
VINRGGTFLG SARFPQFREV EVREKAIENL KKHGIEALVV IGGDGSYMGA KKLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IAGTDYTIGY LTALNTVIEA IDRLRDTSSS HQRISIVEIM GRHCGDLTLT 

       190        200        210        220        230        240 
SAIAGGCEYI ITPETGLNME QLISNIKDGI AKGKKHAIIA LTELMMDANK LAKEIESATG 

       250        260        270        280        290        300 
RETRATVLGH IQRGGKPTAF DRVLASRMGN YAVHLLMEGH GGRCVGIQKE QLVHHDIIDA 

       310        320 
IENMKRPVRT DLYKVAEELF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF95830.1. Different initiation.
PIRG82045.
RefSeqNP_232317.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KNP2.
SMRQ9KNP2. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC2689.

Proteomic databases

PRIDEQ9KNP2.

Protocols and materials databases

DNASU2615517.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95830; AAF95830; VC_2689.
GeneID2615517.
KEGGvch:VC2689.
PATRIC20084396. VBIVibCho83274_2564.

Phylogenomic databases

eggNOGCOG0205.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_VIBCH
AccessionPrimary (citable) accession number: Q9KNP2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways