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Q03216 (PFKA2_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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 subunit beta

Short name=ATP-PFK 2
Short name=Phosphofructokinase 2
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 2
Gene names
Name:PFK2
Ordered Locus Names:KLLA0F06248g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Heterooctamer of 4 alpha and 4 beta chains.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 938938ATP-dependent 6-phosphofructokinase subunit beta HAMAP-Rule MF_03184
PRO_0000112041

Regions

Nucleotide binding249 – 2502ATP By similarity
Nucleotide binding279 – 2824ATP By similarity
Region1 – 552552N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region325 – 3273Substrate binding By similarity
Region369 – 3713Substrate binding By similarity
Region460 – 4634Substrate binding By similarity
Region553 – 56614Interdomain linker HAMAP-Rule MF_03184
Region567 – 938372C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region695 – 6995Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region740 – 7423Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region832 – 8354Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3271Proton acceptor By similarity
Metal binding2801Magnesium; catalytic By similarity
Binding site1851ATP; via amide nitrogen By similarity
Binding site3621Substrate; shared with subunit alpha By similarity
Binding site4261Substrate By similarity
Binding site4541Substrate; shared with subunit alpha By similarity
Binding site6371Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7331Allosteric activator fructose 2,6-bisphosphate; shared with subunit alpha By similarity
Binding site8261Allosteric activator fructose 2,6-bisphosphate; shared with subunit alpha By similarity
Binding site9151Allosteric activator fructose 2,6-bisphosphate By similarity

Experimental info

Sequence conflict5231Missing in CAA78964. Ref.1
Sequence conflict5541D → H in CAA78964. Ref.1
Sequence conflict783 – 7842FS → LR in CAA78964. Ref.1
Sequence conflict927 – 93812TIADH…GRKKL → PLRTICRKEKTYEIKNVSAS SKFPLKWMYIIM in CAA78964. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03216 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: CE9C56DD7588C955

FASTA938102,477
        10         20         30         40         50         60 
MTQSLPLLNG TEAYKLVTTQ GLYDKTVKFY EKYLQLVHDK RVGTLTNSLI TLKLVVDNSF 

        70         80         90        100        110        120 
KPLDVVNDKD WRAIVSSALV FSCTNIQHFR DLAAGETIQA YPNETNPIEI YLKDPNGYII 

       130        140        150        160        170        180 
GITETKNAIS IKPTLPKQSV EASLISSRSS RIDIASSGVS TDSSYPAIPK TAKAQKSIAV 

       190        200        210        220        230        240 
MTSGGDAPGM NANVRAIVRT AIFKGCNAFV VMEGYEGLVK GGPNYIKQVY WETVRNWSCE 

       250        260        270        280        290        300 
GGTNIGTARC KEFREREGRL LGALHLIEAG VDALIVCGGD GSLTGADLFR SEWPSLIREL 

       310        320        330        340        350        360 
LDQGRINKVQ FDRYQHLNIC GTVGSIDNDM STTDATIGAY SALDRICQAI DYIEATANSH 

       370        380        390        400        410        420 
SRAFVVEVMG RNCGWLALLA GISTSADYIL IPEKPASSRE WQDQMCDIIS KHRSRGKRTT 

       430        440        450        460        470        480 
IVIVAEGAIS ADLTPISSKD VHKVLVDRLG LDCRITTLGH VQRGGTAVAY DRILATLQGV 

       490        500        510        520        530        540 
EAVNAVLEST PDTPSPLIAI NENKITRKPL VESVQLTKSV AEAIHSKDFK KAMQLRDSEF 

       550        560        570        580        590        600 
VEHLDNFMAI NSADHIEPKL PEHTHMKIAI VNVGAPAGGM NSAVYSMATY CMSQGHKPYA 

       610        620        630        640        650        660 
IYNGWTGLTR HESVRSLNWK DLLGWQSRGG SEIGTNRHTP EEADIGLIAY YFQKYGFDGI 

       670        680        690        700        710        720 
IIVGGFEAFV SLHQLERARE NYTAFRIPMV LIPATLSNNV PGTEYSLGSD TALNSLMQYC 

       730        740        750        760        770        780 
DIIKQSAAST RGRVFVVDVQ GGNSGYLATH AAVAVGAQVS YVPEEGISLE QLTQDIENLT 

       790        800        810        820        830        840 
ESFSEAEGRG KFGQLILKST NASKVLTPEV LAEVITQEAE GHFDAKCAIP GHVQQGGLPS 

       850        860        870        880        890        900 
PIDRTRGTRF AIRAVGFIES QHKVLAAEAN LDDDDFDFDT PKIIATASVL GVKGSDIVFS 

       910        920        930 
SIRQLYDFET ELNKRTPKTI HWQSTRTIAD HLVGRKKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z17316 Genomic DNA. Translation: CAA78964.1.
CR382126 Genomic DNA. Translation: CAG98071.1.
PIRS32903.
RefSeqXP_455363.1. XM_455363.1.

3D structure databases

ProteinModelPortalQ03216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q03216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2894998.
KEGGkla:KLLA0F06248g.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAHKPYAIY.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

SABIO-RKQ03216.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA2_KLULA
AccessionPrimary (citable) accession number: Q03216
Secondary accession number(s): Q6CL26
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways