ID U5W531_9ACTN Unreviewed; 435 AA.
AC U5W531;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=pfkA {ECO:0000256|HAMAP-Rule:MF_01981};
GN ORFNames=AFR_30340 {ECO:0000313|EMBL:AGZ44328.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ44328.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ44328.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ44328.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ44328.1; -; Genomic_DNA.
DR RefSeq; WP_023560665.1; NC_022657.1.
DR AlphaFoldDB; U5W531; -.
DR STRING; 1246995.AFR_30340; -.
DR KEGG; afs:AFR_30340; -.
DR PATRIC; fig|1246995.3.peg.6143; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_7_4_11; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000017746; 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: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:UP000017746};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01981}.
FT DOMAIN 77..381
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 151..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 176..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 250..252
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 356..359
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT SITE 178
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ SEQUENCE 435 AA; 46613 MW; F44571C452338A14 CRC64;
MVDPGQLIVR SLGESRIPSP LGSLLTRRGT TEHYVDEADR VLLDDTVAML AARGDELPSF
EPGGPRRRIY FDPSKIRAGI VTCGGLCPGL NDVIRGLVLT LNNQYGVSRI LGFRNGYQGL
TPGAGHSVVE LTPAGVEYIN EHGGTILGTS RGNQDPEEIV DCLEQLGVNL LFVVGGDGSM
RGARLISETI AARDRRIAVV GVPKTIDNDI PYIGQSFGFQ TAYAKAAESI RAAHVEAAAQ
PSGVGLVQLM GRHSGFIASY AALANNDADY VLIPEVPFSL DGFLPALRRR VADRGHALVV
VAEGAGQEHL RDAPLRLDAS GNRKLGDFGL HLRDRILDDF AAAAREVNLK YIDPSYAIRS
VPANPYDSVY CLRLAQAAVH AAMAGRTELV VGMWRGRFVH VPIPLAVSGR NQVDPDGDLW
LSVLEATGQP PDFTA
//
