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Q92448 (PFKA1_PICPG) 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 alpha

EC=2.7.1.11
Alternative name(s):
ATP-dependent 6-phosphofructokinase 1
Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
Glucose-induced selective autophagy 1 protein
Phosphohexokinase 1
Gene names
Name:PFK1
Synonyms:GSA1
Ordered Locus Names:PAS_chr2-1_0402
OrganismKomagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) [Reference proteome]
Taxonomic identifier644223 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKomagataella

Protein attributes

Sequence length989 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 By similarity. Involved in the modulation of glucose-induced microautophagy of peroxisomes independent of its ability to metabolize glucose intermediates. Ref.1

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

Heterododecamer of 4 alpha, 4 beta and 4 gamma chains. The gamma chain bridges the N-terminal halves of the alpha and beta subunits 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 989989ATP-dependent 6-phosphofructokinase subunit alpha HAMAP-Rule MF_03184
PRO_0000112042

Regions

Nucleotide binding283 – 2842ATP By similarity
Nucleotide binding313 – 3164ATP By similarity
Region1 – 585585N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region359 – 3613Substrate binding By similarity
Region403 – 4053Substrate binding By similarity
Region493 – 4964Substrate binding By similarity
Region586 – 59914Interdomain linker HAMAP-Rule MF_03184
Region600 – 989390C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region727 – 7315Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region772 – 7743Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region864 – 8674Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3611Proton acceptor By similarity
Metal binding3141Magnesium; catalytic By similarity
Binding site2201ATP; via amide nitrogen By similarity
Binding site3961Substrate; shared with subunit beta By similarity
Binding site4601Substrate By similarity
Binding site4871Substrate; shared with subunit beta By similarity
Binding site6701Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7651Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site8321Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8581Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site9631Allosteric activator fructose 2,6-bisphosphate By similarity

Experimental info

Mutagenesis3611D → S: Abolishes catalytic activity, but not the ability to modulate glucose-induced microautophagy of peroxisomes. Ref.1
Sequence conflict1781S → SK in AAB97871. Ref.1
Sequence conflict5701D → E in AAB97871. Ref.1
Sequence conflict9141Y → C in AAB97871. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q92448 [UniParc].

Last modified July 9, 2014. Version 2.
Checksum: 6708A34ED94C9DD4

FASTA989108,817
        10         20         30         40         50         60 
MPEPSISALS FTSFVTNDDK LFEETFNFYT KLGFHATRSY VKDNRSDFEL TGISTDSIKE 

        70         80         90        100        110        120 
IWLESFPLSE VVETSAGREL RKPLQESVGY QSEALLGYSP YQSDGVVIKL RLSNHDLQKN 

       130        140        150        160        170        180 
KDLPGEVTFF TASIDKLRAK LIEIGAEIIP SEIDLVEFST KDPMGDVISF SSYPSLSSKK 

       190        200        210        220        230        240 
ITSPDFFLHP KKEVRSQESI VEQVKSEEGK KKIAIITSGG DAPGMNAAVR AVTRAGIFYG 

       250        260        270        280        290        300 
CKVYACYEGY TGLVKGGDML KELQWQDVRG LLSIGGTIIG TARSKEFRER WGRLQACYNM 

       310        320        330        340        350        360 
VSNGIDALVV CGGDGSLTGA DLFRNEWPEL IKELLGEGKI TKEQYETHRN LTIVGLVGSI 

       370        380        390        400        410        420 
DNDMCGTDST IGAYSSLERI IELVDYIDAT AASHSRAFVV EVMGRHCGWL GLMSGIATGA 

       430        440        450        460        470        480 
DYIFIPERPP SETNWKDDLK KVCLRHREKG RRKTTVIVAE GAIDDQLNPI TSEEVKDVLV 

       490        500        510        520        530        540 
EIGLDTRITR LGHVQRGGAP CAFDRFLATV QGVDAVRAVL ESTPAIPSPV ISILENKIVR 

       550        560        570        580        590        600 
QPLVESVAQT KTVSDAIEAK DFDKALKLRD QEFATSYESF LSVSKYDDGS YLVPESSRLN 

       610        620        630        640        650        660 
IAIIHVGAPT SALNPATRVA TLNSLAKGHR VFAIRNGFAG LIRHGAVREL NWIDVEDWHN 

       670        680        690        700        710        720 
TGGSEIGTNR SLPSDDMGTV AYYFQQYKFD GLIIIGGFEA FTALYQLDAA RAQYPIFNIP 

       730        740        750        760        770        780 
MCCLPATVSN NVPGTEYSLG SDTCLNTLSG YCDAVKQSAS ASRRRTFVVE VQGGYSGYLA 

       790        800        810        820        830        840 
SYAGLITGAL AVYTPENPIN LQTVQEDIEL LTRTYEEDDG KNRSGKIFIH NEKASKVYTT 

       850        860        870        880        890        900 
DLIAAIIGEA GKGRFESRTA VPGHVQQGKS PSSIDRVNAC RLAIKCCNFI EDANFQVKHN 

       910        920        930        940        950        960 
ANLSADERHL RFFYDDGVKT SAVSGKSSVI DDNTSVVIGI QGSEVTFTPV KQLWEKETHH 

       970        980 
KWRKGKNVHW EQLNIVSDLL SGRLSIRTT 

« Hide

References

« Hide 'large scale' references
[1]"Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase."
Yuan W., Tuttle D.L., Shi Y.J., Ralph G.S., Dunn W.A. Jr.
J. Cell Sci. 110:1935-1945(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ASP-361.
Strain: GS115 / ATCC 20864.
[2]"Genome sequence of the recombinant protein production host Pichia pastoris."
De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S., Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.
Nat. Biotechnol. 27:561-566(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS115 / ATCC 20864.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73376 Genomic DNA. Translation: AAB97871.1.
FN392320 Genomic DNA. Translation: CAY69023.1.

3D structure databases

ProteinModelPortalQ92448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING644223.PAS_chr2-1_0402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

KEGGppa:PAS_chr2-1_0402.

Phylogenomic databases

eggNOGCOG0205.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

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. 3 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA1_PICPG
AccessionPrimary (citable) accession number: Q92448
Secondary accession number(s): C4R0J9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 9, 2014
Last modified: July 9, 2014
This is version 75 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