ID A0A1M4W940_9BACT Unreviewed; 550 AA.
AC A0A1M4W940;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01980};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01980};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01980};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01980};
GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01980};
GN ORFNames=SAMN05444274_102368 {ECO:0000313|EMBL:SHE77754.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE77754.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHE77754.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE77754.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01980}.
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|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC Rule:MF_01980};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01980};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01980}.
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_01980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01980}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01980}.
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DR EMBL; FQUM01000002; SHE77754.1; -; Genomic_DNA.
DR RefSeq; WP_072999520.1; NZ_FQUM01000002.1.
DR AlphaFoldDB; A0A1M4W940; -.
DR STRING; 1484053.SAMN05444274_102368; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000184164; 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; 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 Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02477; PFKA_PPi; 1.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01980};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01980};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01980};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01980}; Reference proteome {ECO:0000313|Proteomes:UP000184164};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01980}.
FT DOMAIN 70..343
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 78
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 200..202
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 239..240
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 247..249
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 308
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT BINDING 424..427
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT SITE 173
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_01980"
FT SITE 199
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
SQ SEQUENCE 550 AA; 60250 MW; C9E2EEB89628DF78 CRC64;
MNISALQKER AKYQPKLPQS LKGAVKLVEG AKTESVADQK EIEELFPNTY GMPLVAFEAG
GADESREPVN VGVILSGGQA PGGHNVISGI FDGIKKINPE SKLYGFLGGP GGLVDHKYVE
LTSAIIDEYR NTGGFDIIGS GRTKLEEEWQ FDKGLEIAKD LKLNALVIIG GDDSNTNACV
LAEYYSQKNA GVQVIGCPKT IDGDLKNEMI ETSFGFDTAT KVYSELIGNI QRDANSAKKY
WHFIKLMGRS ASHIGLECAL KTQPNITLIS EEIAEKKQTL SDIVNYMAAI VARRAGNGEN
FGVALIPEGL IEFVPEMKKL IAELNDLLAE GTDTEKEFKM LRKSHRLDWV ASHLCEDSAN
VFKSLPAGIA TQLTLDRDPH GNVQVSLIET EKLLGEMVAE KLSAMKKAGE FAGKFSTQYH
FFGYEGRCAA PSNFDADYCY SLGYTASLLV SEGKTGYMSS VRNLTAPAEK WIAGGVPVTM
MMNMEKRHGH MKPVIQKALV ELDGKPFKYF VSKRGEWAYG TQYIYPGPIQ YFGPADVCDQ
PTETLNLEKA
//
