ID M5WH94_PRUPE Unreviewed; 568 AA.
AC M5WH94;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_03185};
DE Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185};
GN Name=PFP-BETA {ECO:0000256|HAMAP-Rule:MF_03185};
GN ORFNames=PRUPE_4G014600 {ECO:0000313|EMBL:ONI09863.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI09863.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI09863.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- FUNCTION: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-
CC phosphate, the first committing step of glycolysis. Uses inorganic
CC phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-
CC dependent phosphofructokinases (ATP-PFKs), which renders the reaction
CC reversible, and can thus function both in glycolysis and
CC gluconeogenesis. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC Rule:MF_03185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
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_03185}.
CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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DR EMBL; CM007654; ONI09863.1; -; Genomic_DNA.
DR RefSeq; XP_007211880.1; XM_007211818.1.
DR AlphaFoldDB; M5WH94; -.
DR STRING; 3760.M5WH94; -.
DR EnsemblPlants; ONI09863; ONI09863; PRUPE_4G014600.
DR GeneID; 18779670; -.
DR Gramene; ONI09863; ONI09863; PRUPE_4G014600.
DR KEGG; pper:18779670; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR OMA; SAKKYWH; -.
DR OrthoDB; 197423at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000006882; Chromosome g4.
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:InterPro.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
DR Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02477; PFKA_PPi; 1.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03185}; Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 98..411
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 106
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 228..230
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 267..268
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 275..277
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 441..444
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT SITE 201
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT SITE 227
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
SQ SEQUENCE 568 AA; 61538 MW; 70839F7390294ED6 CRC64;
MTPSLVANGG VAAGEAVAAP VTGRVAAVYS EVQSSRIDHA LPLPSVLTKP FKVVDGPASS
AAGNPDEIAK LFPNVFGQPS ALLVPSDSDS ALPQQKLKIG VVLSGGQAPG GHNVISGIFD
YLQDRAKGST LYGFRGGPAG IMKNKFIELN SEYIYPYRNQ GGFDMICSGR DKIETPEQFK
QAEETAVKLD LDGLVVIGGD DSNTNACLLA ENFRGKNLKT RVIGCPKTID GDLKCKEVPT
SFGFDTACKI YAEMIGNVMI DARSTGKYYH FVRLMGRAAS HITLECALQT HPNITIIGEE
VAAKKQTLKN VTDYIVNIIL KRADLGYNYG VILIPEGLID FIPEVQNLIA ELNEILAHDV
VDEGGLWKNK LTSQSLQLFD FLPEAIQEQL MLERDPHGNV QVAKIETEKM LIQMVETDLE
KRRQEGSYNG QFKGQSHFFG YEGRCGLPTN FDSTYCYALG YGAGALLHSG KTGVISSVGN
LAAPVEEWTV GGTALTSLMD VERRHGKFKP VIKKAMVELE GAPFKKFASL RNDWAINNRY
ISPGPIQFHG PASNALSHTL LLELGVQA
//
