PFPB_SOLTU
ID PFPB_SOLTU Reviewed; 569 AA.
AC P21343; M1BE40;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 03-AUG-2022, entry version 129.
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};
GN ORFNames=PGSC0003DMG400016726;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 410-421.
RC STRAIN=cv. Kennebec;
RX PubMed=2170409; DOI=10.1016/s0021-9258(17)44761-2;
RA Carlisle S.M., Blakeley S.D., Hemmingsen S.M., Trevanion S.J., Hiyoshi T.,
RA Kruger N.J., Dennis D.T.;
RT "Pyrophosphate-dependent phosphofructokinase. Conservation of protein
RT sequence between the alpha- and beta-subunits and with the ATP-dependent
RT phosphofructokinase.";
RL J. Biol. Chem. 265:18366-18371(1990).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS, AND IDENTIFICATION OF FRAMESHIFTS.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63452.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M55191; AAA63452.1; ALT_FRAME; mRNA.
DR PIR; B36094; B36094.
DR RefSeq; NP_001275324.1; NM_001288395.1.
DR AlphaFoldDB; P21343; -.
DR SMR; P21343; -.
DR STRING; 4113.PGSC0003DMT400043111; -.
DR PRIDE; P21343; -.
DR EnsemblPlants; PGSC0003DMT400043111; PGSC0003DMT400043111; PGSC0003DMG400016726.
DR EnsemblPlants; RHC02H1G1959.2.1; RHC02H1G1959.2.1; RHC02H1G1959.2.
DR EnsemblPlants; RHC02H1G1962.2.1; RHC02H1G1962.2.1; RHC02H1G1962.2.
DR GeneID; 102577862; -.
DR Gramene; PGSC0003DMT400043111; PGSC0003DMT400043111; PGSC0003DMG400016726.
DR Gramene; RHC02H1G1959.2.1; RHC02H1G1959.2.1; RHC02H1G1959.2.
DR Gramene; RHC02H1G1962.2.1; RHC02H1G1962.2.1; RHC02H1G1962.2.
DR KEGG; sot:102577862; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR OMA; SAKKYWH; -.
DR OrthoDB; 347054at2759; -.
DR SABIO-RK; P21343; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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:0008443; F:phosphofructokinase activity; IBA:GO_Central.
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; 3.40.50.460; -; 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 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..569
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit beta"
FT /id="PRO_0000112050"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 107
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 229..231
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 268..269
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 276..278
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 337
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 442..445
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 202
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 228
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"
FT CONFLICT 437
FT /note="S -> F (in Ref. 1; AAA63452)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="W -> L (in Ref. 1; AAA63452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 61868 MW; 93D68700BA3F2FFD CRC64;
MAAATLSLLN NGELASSVKS PGTGRYAAVY SEVQNSRLDH PLPLPSVLGS PFKVVDGPPS
SAAGHPEEIA KLFPSLYGQP CVSLVPDDSG DVAMNQILKI GVVLSGGQAP GGHNVISGIF
DYLQTHCKGS TMYGFRGGPA GVMKGKYVVL TPEFIYPYRN QGGFDMICSG RDKIETPEQF
KQAEETAKKL DLDGLVVIGG DDSNTNACLL AENFRSKNLK TRVIGCPKTI DGDLKSKEVP
TSFGFDTACK IYAEMIGNVM IDARSTGKYY HFVRLMGRAA SHITLECALQ THPNVTLIGE
EVFAKKLTLK NVTDYIADVV CKRAESGYNY GVILIPEGLI DFIPEVQQLI AELNEILAHD
VVDEAGVWKK KLTPQCLELF ELLPLAIQEQ LLLERDPHGN VQVAKIETEK MLIQMVETEL
DQRKQKGAYN AQFKGQSHFF GYEGRCGLPS NFDSTYCYAL GYGAGSLLQS GKTGLISSVG
NLAAPVEEWT VGGTALTALM DVERRHGKFK PVIKKAMVEL EGAPFKKFAS KREEWALNNR
YINPGPIQFV GPVANKVNHT LLLELGVDA
