ID E4MDV5_9BACT Unreviewed; 411 AA.
AC E4MDV5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Phosphofructokinase {ECO:0000313|EMBL:EFR56909.1};
GN ORFNames=HMPREF9720_1126 {ECO:0000313|EMBL:EFR56909.1};
OS Alistipes sp. HGB5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR56909.1, ECO:0000313|Proteomes:UP000002960};
RN [1] {ECO:0000313|EMBL:EFR56909.1, ECO:0000313|Proteomes:UP000002960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR56909.1,
RC ECO:0000313|Proteomes:UP000002960};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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}.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC {ECO:0000256|ARBA:ARBA00038478}.
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:EFR56909.1}.
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DR EMBL; AENZ01000065; EFR56909.1; -; Genomic_DNA.
DR RefSeq; WP_009598504.1; NZ_AENZ01000065.1.
DR AlphaFoldDB; E4MDV5; -.
DR GeneID; 79837687; -.
DR PATRIC; fig|908612.3.peg.2351; -.
DR eggNOG; COG0205; Bacteria.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002960; Unassembled WGS sequence.
DR GO; GO:0003872; F:6-phosphofructokinase activity; 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 InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFR56909.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..326
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 411 AA; 45340 MW; 461D007EC4168206 CRC64;
MKEAIAILTG GGPAPGMNTV VGSVAKTFLR KGYRVIGLHE GYTGLFNPSP RTVDIDYPMA
DGIFNQGGSF LQMSRFKPKD SDFENNFNLK FFTDNNIKLL VTVGGDDTAS TANRIAKFLE
AKKYPIANIH VPKTIDNDLP LPKGTPTFGY ESAKDKGAVI ARAVYVDART SGNWFVLAAM
GRSAGHLAFG IGEACHYPMI VIPEMFDKTE ITVEKIVNLV ISSIIKRKIM GMDYGAAVIS
EGVFHALSDE EIRKSGIHFT YDEHGHPELG KVSKAHIFNE MIEKKVKELG IKVKSRPVEL
GYEIRCQTPI AYDLTYCSEL GIGVHKLFAE GKTGCMVYVD SEGNVSPLYL KDLQDPTTGK
IPPRLVDIKS DKFSSVVETI LNAITPADYE AAKQYVPNPE EYDFHKILNW K
//
