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Database: UniProt
Entry: Q9L1L8
LinkDB: Q9L1L8
Original site: Q9L1L8 
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   12-SEP-2018, entry version 116.
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.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor 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;
RA   Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L.;
RT   "Identification of ATP-dependent phosphofructokinase as a regulatory
RT   step in the glycolytic pathway of the actinomycete Streptomyces
RT   coelicolor 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
RT   by phosphofructokinase deletion.";
RL   J. Biol. Chem. 283:25186-25199(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to 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: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_01976,
CC       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
CC       phosphoenolpyruvate. {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-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- DISRUPTION PHENOTYPE: Accumulates glucose 6-phosphate and fructose
CC       6-phosphate. Has an increased carbon flux through the pentose
CC       phosphate pathway, resulting in a higher production of the
CC       pigmented antibiotics actinorhodin and undecylprodigiosin.
CC       {ECO:0000269|PubMed:18606812}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- CAUTION: The nucleotide sequence reported in PubMed:9055413 was
CC       not that of the characterized enzyme. Inspection of the original
CC       N-terminal sequence showed that the characterized enzyme was pfkA2
CC       (SCO5426) and not pfkA1 (SCO2119), another isozyme in S.coelicolor
CC       (PubMed:18606812). {ECO:0000305|PubMed:18606812}.
DR   EMBL; AL939123; CAB72402.1; -; Genomic_DNA.
DR   RefSeq; NP_629564.1; NC_003888.3.
DR   RefSeq; WP_003973572.1; NC_003888.3.
DR   ProteinModelPortal; Q9L1L8; -.
DR   SMR; Q9L1L8; -.
DR   STRING; 100226.SCO5426; -.
DR   PRIDE; Q9L1L8; -.
DR   EnsemblBacteria; CAB72402; CAB72402; CAB72402.
DR   GeneID; 1100866; -.
DR   KEGG; sco:SCO5426; -.
DR   PATRIC; fig|100226.15.peg.5507; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248869; -.
DR   InParanoid; Q9L1L8; -.
DR   KO; K21071; -.
DR   OMA; GKLHSII; -.
DR   OrthoDB; POG091H01AC; -.
DR   PhylomeDB; Q9L1L8; -.
DR   BRENDA; 2.7.1.11; 5998.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    341       ATP-dependent 6-phosphofructokinase 2.
FT                                /FTId=PRO_0000111987.
FT   NP_BIND      72     73       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   NP_BIND     102    105       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   REGION      125    127       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      169    171       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      272    275       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    127    127       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   METAL       103    103       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      10     10       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     162    162       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     222    222       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING     266    266       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   SITE        104    104       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {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
//
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