ID   PFKA2_STRCO             Reviewed;         341 AA.
AC   Q9L1L8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA2 {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfk2;
GN   OrderedLocusNames=SCO5426; ORFNames=SC6A11.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE OF 1-28, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND ACTIVITY REGULATION.
RC   STRAIN=A3(2) / 1109;
RX   PubMed=9055413; DOI=10.1128/aem.63.3.956-961.1997;
RA   Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L.;
RT   "Identification of ATP-dependent phosphofructokinase as a regulatory step
RT   in the glycolytic pathway of the actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Appl. Environ. Microbiol. 63:956-961(1997).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18606812; DOI=10.1074/jbc.m803105200;
RA   Borodina I., Siebring J., Zhang J., Smith C.P., van Keulen G.,
RA   Dijkhuizen L., Nielsen J.;
RT   "Antibiotic overproduction in Streptomyces coelicolor A3(2) mediated by
RT   phosphofructokinase deletion.";
RL   J. Biol. Chem. 283:25186-25199(2008).
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:0000255|HAMAP-Rule:MF_01976,
CC       ECO:0000269|PubMed:9055413}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01976, ECO:0000269|PubMed:9055413};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01976, ECO:0000269|PubMed:9055413};
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by phosphoenolpyruvate.
CC       {ECO:0000269|PubMed:9055413}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 mM for ATP {ECO:0000269|PubMed:9055413};
CC         Vmax=165 umol/min/mg enzyme {ECO:0000269|PubMed:9055413};
CC       pH dependence:
CC         Optimum pH is 7.5-8. {ECO:0000269|PubMed:9055413};
CC       Temperature dependence:
CC         Optimum temperature is 30-50 degrees Celsius.
CC         {ECO:0000269|PubMed:9055413};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- DISRUPTION PHENOTYPE: Accumulates glucose 6-phosphate and fructose 6-
CC       phosphate. Has an increased carbon flux through the pentose phosphate
CC       pathway, resulting in a higher production of the pigmented antibiotics
CC       actinorhodin and undecylprodigiosin. {ECO:0000269|PubMed:18606812}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01976}.
CC   -!- CAUTION: The nucleotide sequence reported in PubMed:9055413 was not
CC       that of the characterized enzyme. Inspection of the original N-terminal
CC       sequence showed that the characterized enzyme was pfkA2 (SCO5426) and
CC       not pfkA1 (SCO2119), another isozyme in S.coelicolor (PubMed:18606812).
CC       {ECO:0000305|PubMed:18606812}.
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DR   EMBL; AL939123; CAB72402.1; -; Genomic_DNA.
DR   RefSeq; NP_629564.1; NC_003888.3.
DR   RefSeq; WP_003973572.1; NZ_VNID01000011.1.
DR   AlphaFoldDB; Q9L1L8; -.
DR   SMR; Q9L1L8; -.
DR   STRING; 100226.gene:17763078; -.
DR   PaxDb; 100226-SCO5426; -.
DR   PATRIC; fig|100226.15.peg.5507; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_0_0_11; -.
DR   InParanoid; Q9L1L8; -.
DR   OrthoDB; 9802503at2; -.
DR   PhylomeDB; Q9L1L8; -.
DR   BRENDA; 2.7.1.11; 5998.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02483; PFK_mixed; 1.
DR   PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..341
FT                   /note="ATP-dependent 6-phosphofructokinase 2"
FT                   /id="PRO_0000111987"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         72..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         102..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         125..127
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         169..171
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         272..275
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   SITE            104
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ   SEQUENCE   341 AA;  36434 MW;  6C0B09B76FE90BBD CRC64;
     MRIGVLTAGG DCPGLNAVIR SVVHRAVDNY GDEVIGFEDG YAGLLDGRYR ALDLNAVSGI
     LARGGTILGS SRLERDRLRE ACENAGDMIQ NFGIDALIPI GGEGTLTAAR MLSDAGLPVV
     GVPKTIDNDI SSTDRTFGFD TAVGVATEAM DRLKTTAESH QRVMVVEVMG RHAGWIALES
     GMAAGAHGIC LPERPFDPAD LVKMVEERFS RGKKFAVVCV AEGAHPAEGS MDYGKGAIDK
     FGHERFQGIG TALAFELERR LGKEAKPVIL GHVQRGGVPT AYDRVLATRF GWHAVEAAHR
     GDFGRMTALR GTDVVMVPLA EAVTELKTVP KDRMDEAESV F
//