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   27-MAR-2024, entry version 150.
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 /
RC   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; Evidence={ECO:0000255|HAMAP-
CC         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; 284590.Q03216; -.
DR   PaxDb; 284590-Q03216; -.
DR   GeneID; 2894998; -.
DR   KEGG; kla:KLLA0_F06248g; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   HOGENOM; CLU_011053_0_0_1; -.
DR   InParanoid; Q03216; -.
DR   OMA; EWQDQMC; -.
DR   SABIO-RK; Q03216; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00764; Eukaryotic_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 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   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
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
//