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ATP-dependent 6-phosphofructokinase subunit alpha (ATP-PFK 1) (Phosphofructokinase 1) (EC 2.7.1.11) (Phosphohexokinase 1)

 PFKA1_KLULA             Reviewed;         992 AA.
Q03215;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
12-SEP-2018, entry version 124.
RecName: Full=ATP-dependent 6-phosphofructokinase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03184};
Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03184};
Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
Name=PFK1; OrderedLocusNames=KLLA0A05544g;
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. {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- 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; Z17315; CAA78963.1; -; Genomic_DNA.
EMBL; CR382121; CAH02833.1; -; Genomic_DNA.
PIR; S32902; S32902.
RefSeq; XP_451245.1; XM_451245.1.
ProteinModelPortal; Q03215; -.
SMR; Q03215; -.
STRING; 284590.XP_451245.1; -.
PRIDE; Q03215; -.
EnsemblFungi; CAH02833; CAH02833; KLLA0_A05544g.
GeneID; 2896656; -.
KEGG; kla:KLLA0A05544g; -.
eggNOG; KOG2440; Eukaryota.
eggNOG; COG0205; LUCA.
HOGENOM; HOG000200154; -.
InParanoid; Q03215; -.
KO; K00850; -.
OMA; KQYDELC; -.
OrthoDB; EOG092C0LOE; -.
SABIO-RK; Q03215; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000598; Chromosome A.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
GO; GO:0051453; P:regulation of intracellular pH; IEA:EnsemblFungi.
HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
InterPro; IPR009161; 6-Pfructokinase_euk.
InterPro; IPR022953; ATP_PFK.
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; 3.
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 1 992 ATP-dependent 6-phosphofructokinase
subunit alpha.
/FTId=PRO_0000112040.
NP_BIND 256 257 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
NP_BIND 286 289 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
REGION 1 558 N-terminal catalytic PFK domain 1.
REGION 332 334 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 376 378 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 466 469 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 559 572 Interdomain linker.
REGION 573 992 C-terminal regulatory PFK domain 2.
REGION 700 704 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 745 747 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 837 840 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
ACT_SITE 334 334 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03184}.
METAL 287 287 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 193 193 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 369 369 Substrate; shared with subunit beta.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 433 433 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 460 460 Substrate; shared with subunit beta.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 643 643 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 738 738 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit beta.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 805 805 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 831 831 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit beta.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 929 929 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
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


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