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O94200 (PFKA2_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. 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

EC=2.7.1.11
Alternative name(s):
ATP-dependent 6-phosphofructokinase 2
Short name=ATP-PFK 2
Short name=Phosphofructokinase 2
Phosphohexokinase 2
Gene names
Name:PFK2
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length946 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 By similarity.

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
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 – 946946ATP-dependent 6-phosphofructokinase subunit beta HAMAP-Rule MF_03184
PRO_0000112039

Regions

Nucleotide binding256 – 2572ATP By similarity
Nucleotide binding286 – 2894ATP By similarity
Region1 – 559559N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region332 – 3343Substrate binding By similarity
Region376 – 3783Substrate binding By similarity
Region467 – 4704Substrate binding By similarity
Region560 – 57314Interdomain linker HAMAP-Rule MF_03184
Region574 – 946373C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region702 – 7065Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region747 – 7493Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region839 – 8424Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3341Proton acceptor By similarity
Metal binding2871Magnesium; catalytic By similarity
Binding site1921ATP; via amide nitrogen By similarity
Binding site3691Substrate; shared with subunit alpha By similarity
Binding site4331Substrate By similarity
Binding site4611Substrate; shared with subunit alpha By similarity
Binding site6441Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8331Allosteric activator fructose 2,6-bisphosphate; shared with subunit alpha By similarity
Binding site9201Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
O94200 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: AEF6167A741D8672

FASTA946104,046
        10         20         30         40         50         60 
MISIVNGTST LSLVAGSVET LNQAINFYTN ILGLSVHSEQ NDWTYLSNDD NKMIVKIQLD 

        70         80         90        100        110        120 
TKSGLSLDQV NDRRTEIIAK LNVTDWRSLD TTSVLKVQNL VALIETLTTF NYTLQITPNE 

       130        140        150        160        170        180 
LYPNEVYCVG PIGYIIGFTA CDEPLTLVPP LQKSHPKPGL VSNLMSKSGS QSRNIEETKA 

       190        200        210        220        230        240 
VRRNIAVMTS GGDSQGMNAA VRAVVRATIF HGSKAFAVQE GYAGLVKGGP EYIKEMKWQD 

       250        260        270        280        290        300 
VRGFLSEGGT NIGTARCMEF KERWGRLKGC KNLIDAGIDG LIVCGGDGSL TGADLFRHEW 

       310        320        330        340        350        360 
PSLIQELKDK GEITNEQFER HKHLYICGMV GSIDNDMAMT DATIGGYSAL ERICRAIDYI 

       370        380        390        400        410        420 
DATANSHSRA FVVEVMGRHC GWLALMAGIA TSADYIFIPE KPASSKDWQD QMCDIVGKHR 

       430        440        450        460        470        480 
AQGKRKTIVI VAEGAITSDL KPITSDEVKD VLVDRLGLDT RITVLGHVQR GGTAVAFDRT 

       490        500        510        520        530        540 
LATLQGVEAV KAILELTPDV PSPLIAIDEN KICRRPLVEA VRITKSVASA IEAKDFEKAM 

       550        560        570        580        590        600 
SLRDHEFKEH LANFMAMNTA NHEKPTLPRE KRKKIAIINI GAPAGGMNSA VYAMATYCMS 

       610        620        630        640        650        660 
RGHTPYAIHN GFAGLSRHES VKSIEWIDIE GWNSIGGSEI GTNRQTPEET DIGMIAHYFE 

       670        680        690        700        710        720 
KYQFDGLIIV GGFEAFVSLE QLERSRAMYP SFRIPMVLIP ATISNNVPGT EYSLGADTCL 

       730        740        750        760        770        780 
NSLMEYCDIV KQSASATRGT AFIIDVQGGN SGYIATFASL ISGAQASYVP EEGISLQQLE 

       790        800        810        820        830        840 
MDINSLREAF AVEQGMTKSG KLIIKSSNAS KVLTPHTLAD IFNDECHGDF DTKTAIPGHV 

       850        860        870        880        890        900 
QQGGLPSPID RSRGDRFAIR AVQFIEDHCD VLAPYRYELD FPIDDKKILN TAAVLGIKSS 

       910        920        930        940 
RLRFTSIRHL FDFETELGRR MPKTIYWNTI RDISDQLVGR TRLDKP 

« Hide

References

[1]"Genetic and biochemical characterization of phosphofructokinase from the opportunistic pathogenic yeast Candida albicans."
Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J.
Eur. J. Biochem. 260:217-226(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007637 Genomic DNA. Translation: CAB38867.1.

3D structure databases

ProteinModelPortalO94200.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0205.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
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.
SSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA2_CANAX
AccessionPrimary (citable) accession number: O94200
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 75 of the entry and version 1 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