ID A0A136KEH2_9BACT Unreviewed; 419 AA.
AC A0A136KEH2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01979};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01979};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01979};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01979};
DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01979};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01979};
GN Name=pfkA {ECO:0000313|EMBL:KXK07792.1};
GN Synonyms=pfp {ECO:0000256|HAMAP-Rule:MF_01979};
GN ORFNames=UZ03_NOB001000168 {ECO:0000313|EMBL:KXK07792.1};
OS Nitrospira sp. OLB3.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXK07792.1, ECO:0000313|Proteomes:UP000070691};
RN [1] {ECO:0000313|EMBL:KXK07792.1, ECO:0000313|Proteomes:UP000070691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB3 {ECO:0000313|EMBL:KXK07792.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) 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_01979}.
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_01979};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01979};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01979}.
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_01979}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01979}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01979}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK07792.1}.
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DR EMBL; JZQY01000009; KXK07792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KEH2; -.
DR STRING; 1617410.UZ03_NOB001000168; -.
DR PATRIC; fig|1617410.3.peg.175; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000070691; 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: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_01979; Phosphofructokinase_II_Short; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
DR NCBIfam; NF041103; PFKA_PPi_Ttgales; 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; PIRSF036482; PPi_PFK_TM0289; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01979};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01979};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01979};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01979};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01979};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01979}.
FT DOMAIN 8..328
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 15
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 181..183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT BINDING 302..305
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
FT SITE 111
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_01979"
FT SITE 134
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01979"
SQ SEQUENCE 419 AA; 45417 MW; 7E491CB0BFB590C1 CRC64;
MSQQRPVVGI LVGGGPAPGI NSVIGAATIR SILGGSDVIG IHDGFKWIME GQTGKVKPLS
IETISRIHFS GGSCLGTARA NPTKKVEHLD ACVATLGQLG VTRLITIGGD DTAFSALKLE
QRAGGRLQVV HVPKTIDNDL DLPHGIPTFG FQTARHIGVE LVKSLMVDAE TTSRWYFVVT
MGRKAGHLAL GIGKAAGATL TMIPEEFQRR PIRLKTLVDT LVGAIIKRLG SGRSDGVAVL
AEGLVEFLDQ QDLEGLEDVE RDQHGHVRLA EINFGFVLKR AVEKELKRLG LKTTIVEKNI
GYELRCADPI SFDMEYTRDL GYCAAQFLLD GGNAAMVSIQ SGRFIPIPFA DILDPATGRT
RVRMVDVESE SYVIARRYMI RLGADDLQQP QDLARHAKIA GLSPDDFRAR FGYLVDKGL
//
