PFP_META2
ID PFP_META2 Reviewed; 409 AA.
AC G4STG9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
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}; OrderedLocusNames=MEALZ_3302;
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;
RX PubMed=22207753; DOI=10.1128/jb.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;
RX PubMed=20868748; DOI=10.1016/j.resmic.2010.09.009;
RA Rozova O.N., Khmelenina V.N., Vuilleumier S., Trotsenko Y.A.;
RT "Characterization of recombinant pyrophosphate-dependent 6-
RT phosphofructokinase from halotolerant methanotroph Methylomicrobium
RT alcaliphilum 20Z.";
RL Res. Microbiol. 161:861-868(2010).
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:20868748}.
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:20868748};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01977,
CC ECO:0000269|PubMed:20868748};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01977,
CC ECO:0000269|PubMed:20868748}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for phosphate {ECO:0000269|PubMed:20868748};
CC KM=0.118 mM for diphosphate {ECO:0000269|PubMed:20868748};
CC KM=0.64 mM for fructose 6-phosphate {ECO:0000269|PubMed:20868748};
CC KM=0.095 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:20868748};
CC KM=1.01 mM for sedoheptulose-7-phosphate
CC {ECO:0000269|PubMed:20868748};
CC Vmax=577 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:20868748};
CC Vmax=805 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:20868748};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20868748};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:20868748};
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: Homotetramer. {ECO:0000269|PubMed:20868748}.
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; FO082060; CCE24967.1; -; Genomic_DNA.
DR RefSeq; WP_014149724.1; NC_016112.1.
DR AlphaFoldDB; G4STG9; -.
DR SMR; G4STG9; -.
DR STRING; 1091494.MEALZ_3302; -.
DR PRIDE; G4STG9; -.
DR EnsemblBacteria; CCE24967; CCE24967; MEALZ_3302.
DR KEGG; mah:MEALZ_3302; -.
DR PATRIC; fig|271065.3.peg.3401; -.
DR HOGENOM; CLU_643544_0_0_6; -.
DR OMA; WFAKQFA; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008315; Chromosome.
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;
KW Reference proteome; Transferase.
FT CHAIN 1..409
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429706"
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; 44437 MW; B0EA8AAFE0CA27F4 CRC64;
MNKPKKVAIL TAGGLAPCLS SAIGSLIERY TEIDPSIEII CYRSGYKGLL LGDSYAVTPK
IRENAALLHK FGGSPIGNSR VKLTNVKDCI KRGLVQEGQD PQKVAADQLV KDGVDVLHTI
GGDDTNTAAA DLAAFLAKND YGLTVIGLPK TIDNDVFPIK QSLGAWTAAE QGAQYFQNVV
AEYNANPRML IVHEVMGRNC GWLTAATAME YRKLLDRSEW LPEIGLDRAA YEVHGVFVPE
MEIDLAAEAK RLREVMDKVD CVNIFVSEGA GVDAIVAEMQ AKGQEVPRDA FGHIKLDAVN
PGKWFGEQFA EMIGAEKTLI QKSGYFARAS ASNVDDIRLI KSCADLAVEC AFRRESGVIG
HDEDNGNVLR AIEFPRIKGG KPFDIDTPWF VQMLAGIGQS KGARVEVSH
