ID A0A239TEF4_9FIRM Unreviewed; 393 AA.
AC A0A239TEF4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=pfkA_1 {ECO:0000313|EMBL:SNU95932.1};
GN Synonyms=pfp {ECO:0000256|HAMAP-Rule:MF_01978};
GN ORFNames=SAMEA4364220_00505 {ECO:0000313|EMBL:SNU95932.1};
OS Megamonas hypermegale.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=158847 {ECO:0000313|EMBL:SNU95932.1, ECO:0000313|Proteomes:UP000215383};
RN [1] {ECO:0000313|EMBL:SNU95932.1, ECO:0000313|Proteomes:UP000215383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10570 {ECO:0000313|EMBL:SNU95932.1,
RC ECO:0000313|Proteomes:UP000215383};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906446; SNU95932.1; -; Genomic_DNA.
DR RefSeq; WP_051177556.1; NZ_LT906446.1.
DR AlphaFoldDB; A0A239TEF4; -.
DR GeneID; 78506536; -.
DR eggNOG; COG0205; Bacteria.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000215383; Chromosome 1.
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:UP000215383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01978}.
FT DOMAIN 10..319
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 18
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 139..141
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 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT SITE 138
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 393 AA; 43109 MW; 3213B5206EF0FCAF CRC64;
MAANVNKIEK IAVVQTGGCS AVINSTLAGI IDNTQKNKLK IYGLLNGFEG LLKDKIIDLS
NLTNDELTRL RNTPAMFLGS SRMFLTAEIF AAIPQKLQEK GIDTLIMIGG NGTMYAAKVI
SESAEKQNIN LTVIGSPKTV DNDMFGIEYS PGFGSAAKYI AQAVRDISID LESMKTFEQV
RIMEVMGRSV GWLAAASALA KRKADGAPHL IYLPEYDFDE NEFLSEVKRV YEEKGFVVAV
VGEGIHDKNG CSIGENPFAD VKQANKTFDG ASTYLANLVH EKLGLKARAQ NLTMAQRCFG
ALRSTVDEER AYKIGFVTIS ALMDGHKSEM VALSDNNVDY YTIALSDVGG KEKKVPVEFY
DVTTKQVTKD FIDWLVPITG EFKDNYLSLD DIN
//
