ID A0A1D8AWB1_9BACT Unreviewed; 409 AA.
AC A0A1D8AWB1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01977};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01977};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01977};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01977};
GN Name=pfp_2 {ECO:0000313|EMBL:AOS45180.1};
GN Synonyms=pfp {ECO:0000256|HAMAP-Rule:MF_01977};
GN ORFNames=Verru16b_02257 {ECO:0000313|EMBL:AOS45180.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS45180.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS45180.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS45180.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01977}.
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:0000256|HAMAP-Rule:MF_01977};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01977};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01977}.
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DR EMBL; CP016094; AOS45180.1; -; Genomic_DNA.
DR RefSeq; WP_069962362.1; NZ_CP016094.1.
DR AlphaFoldDB; A0A1D8AWB1; -.
DR STRING; 1838286.Verru16b_02257; -.
DR KEGG; obg:Verru16b_02257; -.
DR PATRIC; fig|1838286.3.peg.2268; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000095228; 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; 3.40.50.450; -; 1.
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 PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01977};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01977};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01977};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01977}; Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01977}.
FT DOMAIN 6..349
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 14
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 151..153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 196..198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01977"
SQ SEQUENCE 409 AA; 44063 MW; 7D057055FA30A717 CRC64;
MSTKKKVAIL TAGGHAPCLS AAVGQLIVHY TEQCPDWDII CYRSGYKGLL LGQSYVVTPE
VRAQAAGLKN YGGSVIGNSR VKLTNVKDAV KRGLVKEGQL PLTVAAEQLQ KDGVDILHTV
GGDDTNTTAA DLAAYLEKHN YALKVIGLPK TIDNDIIPIR QSLGAVTAAE QGAKFFSNVV
TELGASGRML IVHEVMGRNC GWLTAATASE YQKSLAKQAW VPGLGVTKSR YSVHAIYVPE
MALDIEAEAK RLKALMDSQG NINIFISEGA GLEEIIAELT ASGQEPARDA FGHVRLDTIN
PGKWFAEQFA KKLGAEKVLV QKSGYFARSA PANAEDFKLI DTCVLKAIEC ARAGVSGLIG
HDEERGLELR AIEFPRIKGG KAFDVTQPWF QDLLKEIGQP MTKVVHVAH
//
