GenomeNet

Database: UniProt
Entry: Q03215
LinkDB: Q03215
Original site: Q03215 
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   12-SEP-2018, entry version 124.
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
OS   1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-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
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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   ProteinModelPortal; Q03215; -.
DR   SMR; Q03215; -.
DR   STRING; 284590.XP_451245.1; -.
DR   PRIDE; Q03215; -.
DR   EnsemblFungi; CAH02833; CAH02833; KLLA0_A05544g.
DR   GeneID; 2896656; -.
DR   KEGG; kla:KLLA0A05544g; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000200154; -.
DR   InParanoid; Q03215; -.
DR   KO; K00850; -.
DR   OMA; KQYDELC; -.
DR   OrthoDB; EOG092C0LOE; -.
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:0016471; C:vacuolar proton-transporting V-type ATPase complex; IEA:EnsemblFungi.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
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:InterPro.
DR   GO; GO:0051453; P:regulation of intracellular pH; IEA:EnsemblFungi.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
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; 3.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    992       ATP-dependent 6-phosphofructokinase
FT                                subunit alpha.
FT                                /FTId=PRO_0000112040.
FT   NP_BIND     256    257       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     286    289       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    558       N-terminal catalytic PFK domain 1.
FT   REGION      332    334       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      376    378       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      466    469       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      559    572       Interdomain linker.
FT   REGION      573    992       C-terminal regulatory PFK domain 2.
FT   REGION      700    704       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      745    747       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      837    840       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    334    334       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       287    287       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     193    193       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     369    369       Substrate; shared with subunit beta.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     433    433       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     460    460       Substrate; shared with subunit beta.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     643    643       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     738    738       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with subunit beta.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     805    805       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     831    831       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with subunit beta.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     929    929       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                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
//
DBGET integrated database retrieval system