PFKA2_KLULA
ID PFKA2_KLULA Reviewed; 938 AA.
AC Q03216; Q6CL26;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK2; OrderedLocusNames=KLLA0F06248g;
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.
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; Z17316; CAA78964.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98071.1; -; Genomic_DNA.
DR PIR; S32903; S32903.
DR RefSeq; XP_455363.1; XM_455363.1.
DR AlphaFoldDB; Q03216; -.
DR SMR; Q03216; -.
DR STRING; 28985.XP_455363.1; -.
DR EnsemblFungi; CAG98071; CAG98071; KLLA0_F06248g.
DR GeneID; 2894998; -.
DR KEGG; kla:KLLA0_F06248g; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; Q03216; -.
DR OMA; FEAYHST; -.
DR SABIO-RK; Q03216; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000598; Chromosome F.
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:0003729; F:mRNA binding; IEA:EnsemblFungi.
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:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:EnsemblFungi.
DR CDD; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.10.180.10; -; 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; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
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 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..938
FT /note="ATP-dependent 6-phosphofructokinase subunit beta"
FT /id="PRO_0000112041"
FT REGION 1..552
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 553..566
FT /note="Interdomain linker"
FT REGION 567..938
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 279..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 325..327
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 362
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 369..371
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 426
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 454
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 460..463
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 637
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 695..699
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 733
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 740..742
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 826
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 832..835
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 915
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 alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT CONFLICT 523
FT /note="Missing (in Ref. 1; CAA78964)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="D -> H (in Ref. 1; CAA78964)"
FT /evidence="ECO:0000305"
FT CONFLICT 783..784
FT /note="FS -> LR (in Ref. 1; CAA78964)"
FT /evidence="ECO:0000305"
FT CONFLICT 927..938
FT /note="TIADHLVGRKKL -> PLRTICRKEKTYEIKNVSASSKFPLKWMYIIM (in
FT Ref. 1; CAA78964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 938 AA; 102477 MW; CE9C56DD7588C955 CRC64;
MTQSLPLLNG TEAYKLVTTQ GLYDKTVKFY EKYLQLVHDK RVGTLTNSLI TLKLVVDNSF
KPLDVVNDKD WRAIVSSALV FSCTNIQHFR DLAAGETIQA YPNETNPIEI YLKDPNGYII
GITETKNAIS IKPTLPKQSV EASLISSRSS RIDIASSGVS TDSSYPAIPK TAKAQKSIAV
MTSGGDAPGM NANVRAIVRT AIFKGCNAFV VMEGYEGLVK GGPNYIKQVY WETVRNWSCE
GGTNIGTARC KEFREREGRL LGALHLIEAG VDALIVCGGD GSLTGADLFR SEWPSLIREL
LDQGRINKVQ FDRYQHLNIC GTVGSIDNDM STTDATIGAY SALDRICQAI DYIEATANSH
SRAFVVEVMG RNCGWLALLA GISTSADYIL IPEKPASSRE WQDQMCDIIS KHRSRGKRTT
IVIVAEGAIS ADLTPISSKD VHKVLVDRLG LDCRITTLGH VQRGGTAVAY DRILATLQGV
EAVNAVLEST PDTPSPLIAI NENKITRKPL VESVQLTKSV AEAIHSKDFK KAMQLRDSEF
VEHLDNFMAI NSADHIEPKL PEHTHMKIAI VNVGAPAGGM NSAVYSMATY CMSQGHKPYA
IYNGWTGLTR HESVRSLNWK DLLGWQSRGG SEIGTNRHTP EEADIGLIAY YFQKYGFDGI
IIVGGFEAFV SLHQLERARE NYTAFRIPMV LIPATLSNNV PGTEYSLGSD TALNSLMQYC
DIIKQSAAST RGRVFVVDVQ GGNSGYLATH AAVAVGAQVS YVPEEGISLE QLTQDIENLT
ESFSEAEGRG KFGQLILKST NASKVLTPEV LAEVITQEAE GHFDAKCAIP GHVQQGGLPS
PIDRTRGTRF AIRAVGFIES QHKVLAAEAN LDDDDFDFDT PKIIATASVL GVKGSDIVFS
SIRQLYDFET ELNKRTPKTI HWQSTRTIAD HLVGRKKL
