(data stored in ACNUC7421 zone)

SWISSPROT: Q758H0_ASHGO

ID   Q758H0_ASHGO            Unreviewed;       987 AA.
AC   Q758H0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184};
GN   ORFNames=AGOS_AEL208W {ECO:0000313|EMBL:AAS52477.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52477.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52477.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000256|HAMAP-Rule:MF_03184}.
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:0000256|HAMAP-
CC         Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|PIRNR:PIRNR000533}.
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:0000256|HAMAP-Rule:MF_03184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03184}.
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DR   EMBL; AE016818; AAS52477.1; -; Genomic_DNA.
DR   RefSeq; NP_984653.1; NM_210006.1.
DR   STRING; 33169.AAS52477; -.
DR   EnsemblFungi; AAS52477; AAS52477; AGOS_AEL208W.
DR   GeneID; 4620835; -.
DR   KEGG; ago:AGOS_AEL208W; -.
DR   HOGENOM; HOG000200154; -.
DR   InParanoid; Q758H0; -.
DR   KO; K00850; -.
DR   OMA; RAMQWIT; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0051289; P:protein homotetramerization; IBA:GO_Central.
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; IPR040712; Pfk_N.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   Pfam; PF18468; Pfk_N; 1.
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   3: Inferred from homology;
DR   PRODOM; Q758H0.
DR   SWISS-2DPAGE; Q758H0.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533}.
FT   DOMAIN          8..100
FT                   /note="Pfk_N"
FT                   /evidence="ECO:0000259|Pfam:PF18468"
FT   DOMAIN          210..516
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   DOMAIN          596..886
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NP_BIND         281..282
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   NP_BIND         311..314
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          1..583
FT                   /note="N-terminal catalytic PFK domain 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          198..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..359
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          401..403
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          491..494
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          596..987
FT                   /note="C-terminal regulatory PFK domain 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          723..727
FT                   /note="Allosteric activator fructose 2,6-bisphosphate
FT                   binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          768..770
FT                   /note="Allosteric activator fructose 2,6-bisphosphate
FT                   binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   REGION          860..863
FT                   /note="Allosteric activator fructose 2,6-bisphosphate
FT                   binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   METAL           312
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         218
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         394
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         458
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         485
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         666
FT                   /note="Allosteric activator fructose 2,6-bisphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         761
FT                   /note="Allosteric activator fructose 2,6-bisphosphate;
FT                   shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         828
FT                   /note="Allosteric activator fructose 2,6-bisphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         854
FT                   /note="Allosteric activator fructose 2,6-bisphosphate;
FT                   shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT   BINDING         952
FT                   /note="Allosteric activator fructose 2,6-bisphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
SQ   SEQUENCE   987 AA;  107666 MW;  1005BDFAD44D59F9 CRC64;
     MSVETAYGVA FRSLATTDER LYKATVQFYK RLSFATVKLY DKFKNHGDEM LLSGTSQSSR
     HETWLMSFKL SEVDSSGCRV PQQEAERKLQ SDGAMIKVRL VNEVAAADCG ALRVSYYSGS
     FAEAAAAFPD REEVSEHEFR IRDPLGNEIA LTDTPHLHDA VLGEQAVGAD FFLSGSGETH
     RLAQGRETAA ALMRSLRETP GAPDSKPKKK LAVMTSGGDS PGMNAAVRAV VRAGIYYGCD
     VFAVYEGYEG LLKGGEYLKH MQWSDVRGWL SEGGTLIGTA RCMEFRERKG RKQAAANLIE
     QGIDALVVCG GDGSLTGADL FRSEWPSLVE ELVSDGRFTA QQVHPYRNLT IVGLVGSIDN
     DMSGTDSTIG AYSALERICE MVDYIDATAK SHSRAFVVEV MGRHCGWLAL MAGIATAADY
     IFIPERAAPQ NKWQDEMKEV CRRHKAKGRR NITVIVAEGA LDTELNPITA EQVKTALVEL
     GLDTRITTLG HVQRGGTAVA HDRWLATMQG VDAVKAVLEM TPDTPSPLIG ILEEKIIRIP
     LMESVKLTKQ VAAAIQEKDF DKAISLRDTE FIELYESFIS TTIKDSTAVP ESGPLRVAIV
     HVGAPSAALN AATRAASLYC LANGHKPFAI INGFSGLIQT GEVRELSWID VEDWHNLGGS
     EIGTNRCAAA DDMGAVAYHF QKNEFDGLII IGGFEGFKSL QQLYSARSQY PVFNIPMVMI
     PSTVSNNVPG TEYSLGTDTC LNALVNYTDA IKQSASATRR RVFVVEVQGG HSGYVASFTG
     LVTGAVSVYT PEKKIDLHSI QEDLALLKEN FRHDQGENRN GKLLIRNEQA SSIYTTELIA
     DIIAEQSNGR FGVRTAVPGH VQQGGVPSSK DRVAACRFAV KSVKFLESWN EKAKQAASHD
     DRQLGFRYVK GVKTPMLPNN DASAAVICVN GSTVSFKPVN DLWQNETDVE LRKGHDIHWS
     EFTKVGDILS GRCNLRKEVD AMRAASA
//

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