ID C7REJ6_ANAPD Unreviewed; 406 AA.
AC C7REJ6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=Apre_1588 {ECO:0000313|EMBL:ACV29609.1};
OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV29609.1, ECO:0000313|Proteomes:UP000002294};
RN [1] {ECO:0000313|EMBL:ACV29609.1, ECO:0000313|Proteomes:UP000002294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1
RC {ECO:0000313|Proteomes:UP000002294};
RX PubMed=21304652; DOI=10.4056/sigs.24194;
RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL Stand. Genomic Sci. 1:159-165(2009).
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; CP001708; ACV29609.1; -; Genomic_DNA.
DR RefSeq; WP_015778505.1; NC_013171.1.
DR AlphaFoldDB; C7REJ6; -.
DR STRING; 525919.Apre_1588; -.
DR KEGG; apr:Apre_1588; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_9; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002294; 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01978}.
FT DOMAIN 3..319
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 10
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 111
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 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT SITE 112
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 406 AA; 45559 MW; A084ECA4112BE709 CRC64;
MNCIIAQSGG PTSVINSSLA GVIQGALDNN FDNIYLSLHG IEGIINKDIL EVDKKKFVRG
GVKEKLMARP SSILGSCRFK LPEDLNDDIY KKIFEFLLEK EINVFVYIGG NDSMDTVKKL
NAYILSNNIE GINVIGCPKT IDNDLNGMDH SPGFGSAAKY ICQSLRTIRA DVDIYDLESV
TIVEIMGRHA GWLAASSLLA DFGYHKELVN LVYVPEESKS LKEIEEEVKE KLKTEKNLII
AMAEGFRDTD SYLDKPMFSN SDDGFNHPIV SGVAQRLADY LRDKLGVKSR AVELNIVQRT
SNHISKTDAD EAFKLGYLAL KLGLDKTNLI PVLRRKEGKS YEVFYTEVEP DLIANKEMKI
PESWLKDRKI LREKITAYAL PLIQGEVEQR YENGMPVFVE LSDFTK
//
