PFP_METCA
ID PFP_METCA Reviewed; 420 AA.
AC Q609I3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01978};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01978};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01978};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01978}; OrderedLocusNames=MCA1251;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP COFACTOR.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=19054082; DOI=10.1111/j.1574-6968.2008.01366.x;
RA Reshetnikov A.S., Rozova O.N., Khmelenina V.N., Mustakhimov I.I.,
RA Beschastny A.P., Murrell J.C., Trotsenko Y.A.;
RT "Characterization of the pyrophosphate-dependent 6-phosphofructokinase from
RT Methylococcus capsulatus Bath.";
RL FEMS Microbiol. Lett. 288:202-210(2008).
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_01978, ECO:0000269|PubMed:19054082}.
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_01978,
CC ECO:0000269|PubMed:19054082};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:19054082};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:19054082};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:19054082};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.69 mM for phosphate {ECO:0000269|PubMed:19054082};
CC KM=0.027 mM for diphosphate {ECO:0000269|PubMed:19054082};
CC KM=2.27 mM for fructose 6-phosphate {ECO:0000269|PubMed:19054082};
CC KM=0.328 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:19054082};
CC KM=0.03 mM for sedoheptulose-7-phosphate
CC {ECO:0000269|PubMed:19054082};
CC Vmax=7.6 umol/min/mg enzyme for the forward reaction with fructose 6-
CC phosphate as substrate {ECO:0000269|PubMed:19054082};
CC Vmax=31 umol/min/mg enzyme for the forward reaction with
CC sedoheptulose-7-phosphate as substrate {ECO:0000269|PubMed:19054082};
CC Vmax=9.0 umol/min/mg enzyme for the reverse reaction with fructose
CC 1,6-bisphosphate as substrate {ECO:0000269|PubMed:19054082};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:19054082};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:19054082};
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_01978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:19054082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01978}.
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DR EMBL; AE017282; AAU92465.1; -; Genomic_DNA.
DR RefSeq; WP_010960534.1; NC_002977.6.
DR AlphaFoldDB; Q609I3; -.
DR SMR; Q609I3; -.
DR STRING; 243233.MCA1251; -.
DR EnsemblBacteria; AAU92465; AAU92465; MCA1251.
DR KEGG; mca:MCA1251; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_6; -.
DR OMA; AHDIGYF; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000006821; 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 Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01978; Phosphofructokinase_II_B2; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011404; PPi-PFK_XF0274.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036483; PFK_XF0274; 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..420
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429697"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 13
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT SITE 115
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_01978"
FT SITE 141
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
SQ SEQUENCE 420 AA; 45308 MW; E784A660945FCDEE CRC64;
MAARNAFYAQ SGGVTAVINA SACGVLETAR QYPDRIGTVY AGRNGIVGAL TEDLIDTGQE
SAEAIAALRH TPSGAFGSCR YKLKGLEENR AQYERLIEVF RAHDIGYFFY NGGGDSADTC
LKVSQLSEKL GYPLQAVHIP KTVDNDLPIT DCCPGFGSVA KYIAVSVREA SFDVRSMAAT
STCIFVLEVM GRHAGWIAAA GGLASDERHE LALVILFPEQ VFDPERFLRA VDEKVRSHGY
CSVVVSEGIR GADGRFVAES GSRDVFGHAR LGGVAPVIAD LIKERLGYKY HWAVADYLQR
AARHIASRTD VEQAYAVGKA GVEMALKGLS AVMPAIVRTS DSPYRWEITA ASLAEVANVE
KKMPLEFISA DGFGITEACR RYLRPLIEGE DYPPYAGGLP DYVTLCNVAV PKKLAASFSV
