PFP_METMH
ID PFP_METMH Reviewed; 409 AA.
AC Q3KSV5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01977};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01977};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01977};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01977};
OS Methylomonas methanica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=12;
RX PubMed=16480155; DOI=10.1007/s10628-005-0142-3;
RA Reshetnikov A.S., Mustakhimov I.I., Khmelenina V.N., Beschastny A.P.,
RA Trotsenko Y.A.;
RT "Identification and cloning of the gene encoding pyrophosphate-dependent 6-
RT phosphofructokinase of Methylomonas methanica.";
RL Dokl. Biochem. Biophys. 405:468-470(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RA Beschastny A.P., Sokolov A.P., Khmelenina V.N., Trotsenko Y.A.;
RT "Purification and properties of pyrophosphate-dependent phosphofructokinase
RT of obligate methanotroph Methylomonas methanica.";
RL Biochemistry (Mosc.) 57:1215-1221(1992).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:16480155,
CC ECO:0000269|Ref.2}.
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_01977,
CC ECO:0000269|PubMed:16480155, ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01977};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01977}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for phosphate {ECO:0000269|PubMed:16480155,
CC ECO:0000269|Ref.2};
CC KM=0.051 mM for diphosphate {ECO:0000269|PubMed:16480155,
CC ECO:0000269|Ref.2};
CC KM=0.36 mM for fructose 6-phosphate {ECO:0000269|PubMed:16480155,
CC ECO:0000269|Ref.2};
CC KM=0.1 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16480155,
CC ECO:0000269|Ref.2};
CC Vmax=840 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:16480155, ECO:0000269|Ref.2};
CC Vmax=850 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:16480155, ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16480155, ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16480155, ECO:0000269|Ref.2};
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_01977}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01977}.
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DR EMBL; AY957402; AAY28468.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3KSV5; -.
DR SMR; Q3KSV5; -.
DR PRIDE; Q3KSV5; -.
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: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 HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011405; PPi-PFK_SMc01852.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..409
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429707"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 14
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 151..153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 196..198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT SITE 124
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_01977"
FT SITE 150
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
SQ SEQUENCE 409 AA; 44542 MW; 178BAC424A37F233 CRC64;
MNKPKKVAIL TAGGLAPCLN SAIGSLIERY TEIDPSIEII CYRGGYKGLL LGDSYPVTAE
VRKKAGVLQR FGGSVIGNSR VKLTNVKDCV KRGLVKEGED PQKVAADQLV KDGVDILHTI
GGDDTNTAAA DLAAFLARNN YGLTVIGLPK TVDNDVFPIK QSLGAWTAAE QGARYFMNVV
AENNANPRML IVHEVMGRNC GWLTAATAQE YRKLLDRAEW LPELGLTRES YEVHAVFVPE
MAIDLEAEAK RLREVMDKVD CVNIFVSEGA GVEAIVAEMQ AKGQEVPRDA FGHIKLDAVN
PGKWFGEQFA QMIGAEKTLV QKSGYFARAS ASNVDDMRLI KSCADLAVEC AFRRESGVIG
HDEDNGNVLR AIEFPRIKGG KPFNIDTDWF NSMLSEIGQP KGGKVEVSH
