PFKA1_CANAX
ID PFKA1_CANAX Reviewed; 987 AA.
AC O94201;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=ATP-dependent 6-phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX PubMed=10091602; DOI=10.1046/j.1432-1327.1999.00132.x;
RA Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J.;
RT "Genetic and biochemical characterization of phosphofructokinase from the
RT opportunistic pathogenic yeast Candida albicans.";
RL Eur. J. Biochem. 260:217-226(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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DR EMBL; AJ007638; CAB38868.1; -; Genomic_DNA.
DR AlphaFoldDB; O94201; -.
DR SMR; O94201; -.
DR VEuPathDB; FungiDB:C5_04810W_A; -.
DR VEuPathDB; FungiDB:CAWG_04847; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR040712; Pfk_N.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR Pfam; PF18468; Pfk_N; 1.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..987
FT /note="ATP-dependent 6-phosphofructokinase subunit alpha"
FT /id="PRO_0000112038"
FT REGION 1..602
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 603..616
FT /note="Interdomain linker"
FT REGION 617..987
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 300..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 330..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 376..378
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 413
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 420..422
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 477
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 504
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 510..513
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 686
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 743..747
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 781
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 788..790
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 848
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 874
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 880..883
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 958
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
SQ SEQUENCE 987 AA; 108598 MW; 4EE5BAB6D02349FA CRC64;
MPSSSDAINR ISYISLVTSD NDKFNQTFQF YSQLGFRLTK SFSKVSSYGS GLGANHPEFQ
LGVSHDSLKE VWLESYPLQN VDSNGNLRPW QEMEVYDGDN CERLNESTVI KVRLLGETPL
KSISQKQFVF FTTQLNKIEK ILTDANVKYG KVVDNVILAE DPLNNIISFS NTQNELCKTR
FQSPEEYVEK TTAEILAKRK KSQLGSKFGS FEEISPSEVG GGNGLRKKKI GVMTSGGDAP
GMNPAVRAVV RAGIYYGCDV YAVYEGYEGL VKGGDLLKKM EWSDVRSYMS LGGTSIGTAR
CKEFRERAGR LQGAYNMIKN GIDALVVCGG DGSLTGADLF RSEWPSLVKE LVDTGKLTKE
EVSPYEHLTI VGLVGSIDND MSGTDVTIGA FSALERITEM VDYIGATAAS HSRAFVVEVM
GRHCGWLALL SGLATGADFV FIPERPPKAG LWKEQLKEVC LRHREYGRRK TTVIVAEGAI
DDELNPITSE EVKQVLADLG LDTRNTILGH VQRGGTAVAF DRRLATLQGV EAVKAVLEMT
PDTPSPMIGI LKHKIVRIPL VDAVKQTKAV AEAISNKDFD KAMSLRDNSF YDDYRYFRDI
SIYDDGSKQL SEDKRLNIAI VHVGAASAGL NAATRAVALY SLSRGHKLYA VQDGFAGLVK
GDLKNLTWMD VEGWHSLGGS EIGTNRSLPS QNIGKVAYNL QKFNIQGLLI VGGFEAFTSL
HELSEQKANY PIFEIPMVVV PATVSNNVPG TEYSLGADTC LNQLVSYCDA VQQSASSTRR
RVFVVEVQGG HSGYVASYCG LITGALATYT PESNINLREL QGDIDLLQKV FATDRGEDHN
GTLIVRNEQA SAVYSTQLIA DILKENANKR FETRTAIPGH VQQGFTPSAN DRVMAVKFSL
KAMEFIETRN GCYGKHDRKF SDEEISEHSQ VVIGIHGDVV KFTCIKHLYD NEANVALRKG
KTVHWTDMID VANILNGKSL LKKQERY
