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ATP-dependent 6-phosphofructokinase subunit beta (ATP-PFK 2) (Phosphofructokinase 2) (EC 2.7.1.11) (Phosphohexokinase 2)

 PFKA2_KLULA             Reviewed;         938 AA.
Q03216; Q6CL26;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 2.
12-SEP-2018, entry version 125.
RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
Name=PFK2; OrderedLocusNames=KLLA0F06248g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
PubMed=8326866; DOI=10.1111/j.1365-2958.1993.tb01600.x;
Heinisch J.J., Kirchrath L., Liesen T., Vogelsang K., Hollenberg C.P.;
"Molecular genetics of phosphofructokinase in the yeast Kluyveromyces
lactis.";
Mol. Microbiol. 8:559-570(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
-!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_03184}.
-!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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EMBL; Z17316; CAA78964.1; -; Genomic_DNA.
EMBL; CR382126; CAG98071.1; -; Genomic_DNA.
PIR; S32903; S32903.
RefSeq; XP_455363.1; XM_455363.1.
ProteinModelPortal; Q03216; -.
SMR; Q03216; -.
STRING; 284590.XP_455363.1; -.
PRIDE; Q03216; -.
EnsemblFungi; CAG98071; CAG98071; KLLA0_F06248g.
GeneID; 2894998; -.
KEGG; kla:KLLA0F06248g; -.
eggNOG; KOG2440; Eukaryota.
eggNOG; COG0205; LUCA.
HOGENOM; HOG000200154; -.
InParanoid; Q03216; -.
KO; K00850; -.
OMA; VQEVGWH; -.
OrthoDB; EOG092C0LOE; -.
SABIO-RK; Q03216; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000598; Chromosome F.
GO; GO:0005945; C:6-phosphofructokinase complex; IEA:EnsemblFungi.
GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IEA:EnsemblFungi.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:EnsemblFungi.
Gene3D; 3.10.180.10; -; 1.
HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
InterPro; IPR009161; 6-Pfructokinase_euk.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
InterPro; IPR015912; Phosphofructokinase_CS.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 2.
PIRSF; PIRSF000533; ATP_PFK_euk; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 2.
TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Reference proteome; Transferase.
CHAIN 1 938 ATP-dependent 6-phosphofructokinase
subunit beta.
/FTId=PRO_0000112041.
NP_BIND 249 250 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
NP_BIND 279 282 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
REGION 1 552 N-terminal catalytic PFK domain 1.
REGION 325 327 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 369 371 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 460 463 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 553 566 Interdomain linker.
REGION 567 938 C-terminal regulatory PFK domain 2.
REGION 695 699 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 740 742 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 832 835 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
ACT_SITE 327 327 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03184}.
METAL 280 280 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 185 185 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 362 362 Substrate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 426 426 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 454 454 Substrate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 637 637 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 733 733 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 826 826 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 915 915 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
CONFLICT 523 523 Missing (in Ref. 1; CAA78964).
{ECO:0000305}.
CONFLICT 554 554 D -> H (in Ref. 1; CAA78964).
{ECO:0000305}.
CONFLICT 783 784 FS -> LR (in Ref. 1; CAA78964).
{ECO:0000305}.
CONFLICT 927 938 TIADHLVGRKKL -> PLRTICRKEKTYEIKNVSASSKFPL
KWMYIIM (in Ref. 1; CAA78964).
{ECO:0000305}.
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


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