PFPB_RICCO
ID PFPB_RICCO Reviewed; 552 AA.
AC Q41141;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP {ECO:0000255|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_03185};
GN Name=PFP-BETA {ECO:0000255|HAMAP-Rule:MF_03185};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7835697; DOI=10.1016/0378-1119(94)00646-a;
RA Todd J.F., Blakeley S.D., Dennis D.T.;
RT "Structure of the genes encoding the alpha- and beta-subunits of castor
RT pyrophosphate-dependent phosphofructokinase.";
RL Gene 152:181-186(1995).
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:0000255|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:0000255|HAMAP-Rule:MF_03185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC bisphosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC chains. {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_03185}.
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DR EMBL; Z32850; CAA83683.1; -; Genomic_DNA.
DR PIR; T10107; T10107.
DR AlphaFoldDB; Q41141; -.
DR SMR; Q41141; -.
DR STRING; 3988.XP_002518416.1; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; Q41141; -.
DR UniPathway; UPA00109; UER00182.
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; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..552
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit beta"
FT /id="PRO_0000112049"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 90
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 212..214
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 251..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 259..261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 320
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 425..428
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT SITE 185
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:0000255|HAMAP-Rule:MF_03185"
FT SITE 211
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
SQ SEQUENCE 552 AA; 60114 MW; E4DC19ADB6317A8E CRC64;
MATPNSGRAA SVYSEVQSSR IEHVLPLPSV LNHPFKIVQG PPSSAAGNPD EIAKLFPNLF
GQPSAMLVPD VADSLDSNQQ LKIGLVLSGG QAPGGHNVIS GIFDYLQDRA KGSILYGFRG
GPAGIMKCNY VQLTADYIHP YRNQGGFDMI CSGRDKIETP EQFKQAEETA GKLDLNGLVV
IGGDDSNTNA CLLAENFRSK NLKTRVIGCP KTIDGDLKCK EVPTSFGFDT ACKIYSEMIG
NVMIDARSTG KYYHFVRLMG RAASHITLEC ALQTHPNITI IGEEVAAKKL ALKDVTDYIV
DVICKRADLG YNYGVILIPE GLIDFIPEVQ NLIAELNEIL AHDVVDEGGL WKKKLTSQSL
QLFEFLPVAI QEQLMLERDP HGNVQVAKIE TEKMLIQMVE TELEKRKQQG TYKAHFKGQS
HFFGYEGRCG LPTNFDSTYC YALGYAAGAL LHSGKTGLIS SVGNLGAPVA EWTVGGTALT
SLMDVERRHG KFKPVIKKAM VELEGAPFKK FASLREEWAL KNRYVSPGPI QFMGPGSDAA
SHTLLLELGS VA
