PFKA2_STRCO
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 03-AUG-2022, entry version 134.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976,
CC 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.SCO5426; -.
DR GeneID; 1100866; -.
DR KEGG; sco:SCO5426; -.
DR PATRIC; fig|100226.15.peg.5507; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_0_11; -.
DR InParanoid; Q9L1L8; -.
DR OMA; KFAVICV; -.
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; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02483; PFK_mixed; 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
