ID K0NH72_DESTT Unreviewed; 439 AA.
AC K0NH72;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01981};
GN Name=pfk2 {ECO:0000313|EMBL:CCK80576.1};
GN Synonyms=pfkA {ECO:0000256|HAMAP-Rule:MF_01981};
GN OrderedLocusNames=TOL2_C24150 {ECO:0000313|EMBL:CCK80576.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80576.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK80576.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC Rule:MF_01981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01981};
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_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01981}.
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DR EMBL; FO203503; CCK80576.1; -; Genomic_DNA.
DR RefSeq; WP_014957882.1; NC_018645.1.
DR AlphaFoldDB; K0NH72; -.
DR STRING; 651182.TOL2_C24150; -.
DR KEGG; dto:TOL2_C24150; -.
DR PATRIC; fig|651182.5.peg.2852; -.
DR HOGENOM; CLU_020655_7_4_7; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
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; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01981};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01981};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01981};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01981}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01981}.
FT DOMAIN 78..384
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 152..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 177..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 251..253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 360..363
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT SITE 179
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ SEQUENCE 439 AA; 48272 MW; 508EC6BB7DA37A19 CRC64;
MKNFDFCTDI PTLGEAKIIS PLKKHTKPGE PEKRFISDDA RVIVDVQINR LESDLKKNSS
FDQAGPREKI YFDPSKLKCA IVTCGGLCPG LNDIIRSIVL ELYHIYNVKT IYGIKHGLQG
FIPDFQHDVM NLNPDSVSGI QNTGGSILGS SRGTQDIGMI VDCLERMTIG ILFMVGGDGT
LMASKRIVEE IEQRNLKISV IGIPKTIDND IYLVSRSFGF DTAVDVATLA IKGAHNEAIA
YPNGIGLVKL MGRHSGFLAA TAALAQQDAN FVLIPEVDIS LDGKNGFLQA LENRILHRKH
AVVIVAEGAG QKLFDKQQKK FDPSGNIVLQ DIGLFLKEKI SQWFKAKNIP ISLKYIDPSY
IIRSLPANAN DSVFCGFLGR DAVHAGMAGK TKLLISFWNN HYVHVPMDAA SGKRKNLDPQ
GKLWQSILEA TGQDTFFTD
//
