ID A0A1D9P343_9FIRM Unreviewed; 414 AA.
AC A0A1D9P343;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01978};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01978};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01978};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01978};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01978};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01978};
GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01978};
GN ORFNames=bhn_I1957 {ECO:0000313|EMBL:AOZ96990.1};
OS Butyrivibrio hungatei.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ96990.1, ECO:0000313|Proteomes:UP000179284};
RN [1] {ECO:0000313|Proteomes:UP000179284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA Attwood G.T.;
RT "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT MB2003.";
RL Submitted (OCT-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_01978}.
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_01978};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01978};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01978}.
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_01978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01978}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01978}.
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DR EMBL; CP017831; AOZ96990.1; -; Genomic_DNA.
DR RefSeq; WP_071176637.1; NZ_CP017831.1.
DR AlphaFoldDB; A0A1D9P343; -.
DR KEGG; bhu:bhn_I1957; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000179284; Chromosome i.
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 Gene3D; 3.40.50.460; Phosphofructokinase domain; 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.
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 PIRSF; PIRSF036483; PFK_XF0274; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01978};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01978};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01978};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01978}; Reference proteome {ECO:0000313|Proteomes:UP000179284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01978}.
FT DOMAIN 3..323
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 11
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT SITE 113
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_01978"
FT SITE 139
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
SQ SEQUENCE 414 AA; 45391 MW; 5CDFD280620AE19D CRC64;
MNNVIIGQSG GPTAAINASV AGAYVKAKEL GANKVFGMIH GIEGLLQGEF IDLDKYLSDP
TNVELLKRTP ASVLGTCRYK LPEASVDNSV YKQIFEILDK YNIDSFFYIG GNDSMDTIMK
LSDYSSSHGY DKQFIGIPKT IDNDLPITDH CPGFGSSAKY IATSVKELIR DNQASDPRNP
AIVIVEIMGR NAGWLAAAAS LCTSDDCSGP DAIYLPEIPF DMDDFMNYAK ELSKGHKPAL
IVISEGIKLA DGRYVCELNG NVETDTFGHK QMSAASRVLA DKLTNELGLR TRTVELSTLQ
RSAAHTSSLT DVKEAYQCGV QAVIAANEKK TGKMVIMKRM MENTADYPYI CVYDTYDIHA
IANFEKKVPV EWITDNKRGL TQSFEHYARP LICGEVMPIM SGGLPRHLII PEAL
//
