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Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

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, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATP; via amide nitrogenUniRule annotation
Metal bindingi314 – 3141Magnesium; catalyticUniRule annotation
Active sitei361 – 3611Proton acceptorUniRule annotation
Binding sitei396 – 3961Substrate; shared with subunit betaUniRule annotation
Binding sitei460 – 4601SubstrateUniRule annotation
Binding sitei487 – 4871Substrate; shared with subunit betaUniRule annotation
Binding sitei670 – 6701Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei765 – 7651Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation
Binding sitei832 – 8321Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei858 – 8581Allosteric activator fructose 2,6-bisphosphate; shared with subunit betaUniRule annotation
Binding sitei963 – 9631Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi283 – 2842ATPUniRule annotation
Nucleotide bindingi313 – 3164ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
  3. hydrogen ion transmembrane transport Source: EnsemblFungi
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-phosphofructokinase subunit alphaUniRule annotation (EC:2.7.1.11UniRule annotation)
Alternative name(s):
ATP-dependent 6-phosphofructokinase 1UniRule annotation
Short name:
ATP-PFK 1UniRule annotation
Short name:
Phosphofructokinase 1UniRule annotation
Glucose-induced selective autophagy 1 protein
Phosphohexokinase 1UniRule annotation
Gene namesi
Name:PFK1
Synonyms:GSA1
Ordered Locus Names:PAS_chr2-1_0402
OrganismiKomagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Taxonomic identifieri644223 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella
ProteomesiUP000000314 Componenti: Chromosome 2

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: EnsemblFungi
  2. mitochondrion Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi361 – 3611D → S: Abolishes catalytic activity, but not the ability to modulate glucose-induced microautophagy of peroxisomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 989989ATP-dependent 6-phosphofructokinase subunit alphaPRO_0000112042Add
BLAST

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi644223.PAS_chr2-1_0402.

Structurei

3D structure databases

ProteinModelPortaliQ92448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 585585N-terminal catalytic PFK domain 1Add
BLAST
Regioni359 – 3613Substrate bindingUniRule annotation
Regioni403 – 4053Substrate bindingUniRule annotation
Regioni493 – 4964Substrate bindingUniRule annotation
Regioni586 – 59914Interdomain linkerAdd
BLAST
Regioni600 – 989390C-terminal regulatory PFK domain 2Add
BLAST
Regioni727 – 7315Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni772 – 7743Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni864 – 8674Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
KOiK00850.
OrthoDBiEOG7Q5HPV.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 3 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPSISALS FTSFVTNDDK LFEETFNFYT KLGFHATRSY VKDNRSDFEL
60 70 80 90 100
TGISTDSIKE IWLESFPLSE VVETSAGREL RKPLQESVGY QSEALLGYSP
110 120 130 140 150
YQSDGVVIKL RLSNHDLQKN KDLPGEVTFF TASIDKLRAK LIEIGAEIIP
160 170 180 190 200
SEIDLVEFST KDPMGDVISF SSYPSLSSKK ITSPDFFLHP KKEVRSQESI
210 220 230 240 250
VEQVKSEEGK KKIAIITSGG DAPGMNAAVR AVTRAGIFYG CKVYACYEGY
260 270 280 290 300
TGLVKGGDML KELQWQDVRG LLSIGGTIIG TARSKEFRER WGRLQACYNM
310 320 330 340 350
VSNGIDALVV CGGDGSLTGA DLFRNEWPEL IKELLGEGKI TKEQYETHRN
360 370 380 390 400
LTIVGLVGSI DNDMCGTDST IGAYSSLERI IELVDYIDAT AASHSRAFVV
410 420 430 440 450
EVMGRHCGWL GLMSGIATGA DYIFIPERPP SETNWKDDLK KVCLRHREKG
460 470 480 490 500
RRKTTVIVAE GAIDDQLNPI TSEEVKDVLV EIGLDTRITR LGHVQRGGAP
510 520 530 540 550
CAFDRFLATV QGVDAVRAVL ESTPAIPSPV ISILENKIVR QPLVESVAQT
560 570 580 590 600
KTVSDAIEAK DFDKALKLRD QEFATSYESF LSVSKYDDGS YLVPESSRLN
610 620 630 640 650
IAIIHVGAPT SALNPATRVA TLNSLAKGHR VFAIRNGFAG LIRHGAVREL
660 670 680 690 700
NWIDVEDWHN TGGSEIGTNR SLPSDDMGTV AYYFQQYKFD GLIIIGGFEA
710 720 730 740 750
FTALYQLDAA RAQYPIFNIP MCCLPATVSN NVPGTEYSLG SDTCLNTLSG
760 770 780 790 800
YCDAVKQSAS ASRRRTFVVE VQGGYSGYLA SYAGLITGAL AVYTPENPIN
810 820 830 840 850
LQTVQEDIEL LTRTYEEDDG KNRSGKIFIH NEKASKVYTT DLIAAIIGEA
860 870 880 890 900
GKGRFESRTA VPGHVQQGKS PSSIDRVNAC RLAIKCCNFI EDANFQVKHN
910 920 930 940 950
ANLSADERHL RFFYDDGVKT SAVSGKSSVI DDNTSVVIGI QGSEVTFTPV
960 970 980
KQLWEKETHH KWRKGKNVHW EQLNIVSDLL SGRLSIRTT
Length:989
Mass (Da):108,817
Last modified:July 8, 2014 - v2
Checksum:i6708A34ED94C9DD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781S → SK in AAB97871 (PubMed:9296392).Curated
Sequence conflicti570 – 5701D → E in AAB97871 (PubMed:9296392).Curated
Sequence conflicti914 – 9141Y → C in AAB97871 (PubMed:9296392).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73376 Genomic DNA. Translation: AAB97871.1.
FN392320 Genomic DNA. Translation: CAY69023.1.
RefSeqiXP_002491303.1. XM_002491258.1.

Genome annotation databases

EnsemblFungiiCAY69023; CAY69023; PAS_chr2-1_0402.
GeneIDi8198870.
KEGGippa:PAS_chr2-1_0402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73376 Genomic DNA. Translation: AAB97871.1.
FN392320 Genomic DNA. Translation: CAY69023.1.
RefSeqiXP_002491303.1. XM_002491258.1.

3D structure databases

ProteinModelPortaliQ92448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi644223.PAS_chr2-1_0402.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAY69023; CAY69023; PAS_chr2-1_0402.
GeneIDi8198870.
KEGGippa:PAS_chr2-1_0402.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
KOiK00850.
OrthoDBiEOG7Q5HPV.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 3 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ASP-361.
    Strain: GS115 / ATCC 20864.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GS115 / ATCC 20864.

Entry informationi

Entry nameiPFKA1_PICPG
AccessioniPrimary (citable) accession number: Q92448
Secondary accession number(s): C4R0J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: July 8, 2014
Last modified: March 31, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

External Data

Dasty 3

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 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.