PFKA1_KLULA
ID PFKA1_KLULA Reviewed; 992 AA.
AC Q03215;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit alpha {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 EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK1; OrderedLocusNames=KLLA0A05544g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=8326866; DOI=10.1111/j.1365-2958.1993.tb01600.x;
RA Heinisch J.J., Kirchrath L., Liesen T., Vogelsang K., Hollenberg C.P.;
RT "Molecular genetics of phosphofructokinase in the yeast Kluyveromyces
RT lactis.";
RL Mol. Microbiol. 8:559-570(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {ECO:0000255|HAMAP-Rule:MF_03184}.
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 -!- 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; Z17315; CAA78963.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02833.1; -; Genomic_DNA.
DR PIR; S32902; S32902.
DR RefSeq; XP_451245.1; XM_451245.1.
DR AlphaFoldDB; Q03215; -.
DR SMR; Q03215; -.
DR STRING; 28985.XP_451245.1; -.
DR PRIDE; Q03215; -.
DR EnsemblFungi; CAH02833; CAH02833; KLLA0_A05544g.
DR GeneID; 2896656; -.
DR KEGG; kla:KLLA0_A05544g; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; Q03215; -.
DR OMA; SRYAVKC; -.
DR SABIO-RK; Q03215; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000598; Chromosome A.
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 CDD; cd00764; Eukaryotic_PFK; 1.
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; IPR041914; PFK_vert-type.
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; Reference proteome; Transferase.
FT CHAIN 1..992
FT /note="ATP-dependent 6-phosphofructokinase subunit alpha"
FT /id="PRO_0000112040"
FT REGION 1..558
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 559..572
FT /note="Interdomain linker"
FT REGION 573..992
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 256..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 286..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 332..334
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 369
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 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 433
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 460
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 466..469
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 643
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 700..704
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 738
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 745..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 805
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 831
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 837..840
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 929
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 992 AA; 109336 MW; 724687F850F27F79 CRC64;
MNNSVYGVAF RSLSTGDEKL YKEATRFYHS LGFQTVKLYD NFKNHDDSNL IVGTSKNSVK
ECWLESFKLS ELDSQGFRVP QQEASNQLQT DGVMIKLRLV DTEPLNQTAD TVVYYTVSLD
EVSKIGERVD DHNVKLVDPL GNVVLVTDSH DGKELNASEF IAPKDSSVEQ KITVELVDKD
SKKKKIAVMT SGGDSQGMNA AVRAVVRSSI YYGCDVYAVY EGYEGLVKGG DYLRKMEWKD
VRGWLSEGGT LIGTARSKEF RERWGRKQAC SNLIDQGIDA LVVIGGDGSL TGADLFRSEW
PSLVEELVKD GKFTEDEVAL YQNLTIVGMV GSIDNDMSGT DSTIGAYSAL ERICEMVDYI
DATAKSHSRA FVVEVMGRHC GWLGLMSGIA TAADYIFIPE RAAPHGKWQD ELKRVCQRHR
EKGRRNNTVI VAEGALDDQL NPITAEQVKD VLVELGLDTK ITTLGHVQRG GTAVAHDRWL
ATLQGVDAVK AILNMTPETP SPLIGILENK VIRMPLVESV KLTKQVAAAI EAKDFDKAIS
LRDTEFIELY SNFMSTTVND DGSQLLPEAD RLNIAIVHVG APSAALNAAT RAATLYCLAH
GHRPYAITNG FSGLIQTGQV KELSWIDVED WHNLGGSEIG TNRSVAAEDM GTIAYHFQKN
KFDGVIILGG FEGFKSLKQL RDGRDQYPIF NIPMCLIPAT VSNNVPGTEY SLGSDTCLNA
LVKYTDAIKQ SASSTRRRVF VVEVQGGHSG YVASFTGLVT GAVSVYTPEN AINLKTIQED
LALLKESFKH EQGETRNGKL VIRNEMASDV YTTELLADII TEQSNDRFGV RTAIPGHVQQ
GGVPSSKDRV IASRFAVKCV KFIEQWNKKN TAADNEDFKI LRFNYVNGVK QYTVLDEDLS
AAVICVNGSK ISFKPIAHIW ENETNIELRK GQEIHWEEYN EIGDILSGRS MLRRKIQKEQ
QEESSLPSVA DTPLSSVTVS TSAAKEDSAL YV
