ID A0A0P0SD87_9PSEU Unreviewed; 458 AA.
AC A0A0P0SD87;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AD017_14865 {ECO:0000313|EMBL:ALL82145.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82145.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL82145.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82145.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL82145.1; -; Genomic_DNA.
DR RefSeq; WP_060574588.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SD87; -.
DR STRING; 1096856.AD017_14865; -.
DR KEGG; pecq:AD017_14865; -.
DR PATRIC; fig|1096856.3.peg.3118; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000066228; 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:UP000066228};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01981}.
FT DOMAIN 87..393
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 161..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 186..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 215..217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 260..262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT SITE 188
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ SEQUENCE 458 AA; 49431 MW; 4C9C68A99308F89B CRC64;
MTTWEYSSIT PGDLAIDALG PARITSPLAP LLDARRTTEH YVDAGDRVLL DDTAAGLKAR
GVDVEELPGL EPCGPRRQIY FDPSKTRAGI VTCGGLCPGL NDVIAGLVRT LTYHYGVRRV
VGFRNGYRGF VSSYGHDVVE LTPESVRDIP VDGGTFLGTS RGPQDPEEIV DCLEQMHLNV
LFVIGGDGTM RGAMEIARVV AERGLRIAVV GIPKTIDNDI PFIDQSFGFQ TAFSQASEAI
RSVTVEAKST PGGVGLVKLM GRHSGFIACY ASLVRSDADA VLIPEVPFEL DGETGLLHHL
RRRVEQRGHA VVVVAEGAGQ ELLPPIGRTD ASGNAKLADV GPWLREQISD AFADAGMETT
VRYVDPSYLI RSVPANPYDS VYTVRLSQAA VHAAMSGRTS MVVGRVRRRF VHIPMALAVS
RRNQVDPHGD LWMAVLESTG QPWRFGEDSG APTRAPHT
//
