ID   PFP_PROFR               Reviewed;         404 AA.
AC   P29495;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 57.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase;
DE            EC=2.7.1.90;
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent;
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
DE   AltName: Full=PPi-dependent phosphofructokinase;
DE            Short=PPi-PFK;
GN   Name=pfp; Synonyms=pfk;
OS   Propionibacterium freudenreichii subsp. shermanii.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Propionibacterineae; Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=91358443; PubMed=1653240;
RA   Ladror U.S., Gollapudi L., Tripathi R.L., Latshaw S.P., Kemp R.G.;
RT   "Cloning, sequencing, and expression of pyrophosphate-dependent
RT   phosphofructokinase from Propionibacterium freudenreichii.";
RL   J. Biol. Chem. 266:16550-16555(1991).
RN   [2]
RP   IDENTIFICATION OF CRITICAL LYSYL RESIDUES.
RX   MEDLINE=92273593; PubMed=1317210; DOI=10.1021/bi00135a011;
RA   Green P.C., Latshaw S.P., Ladror U.S., Kemp R.G.;
RT   "Identification of critical lysyl residues in the pyrophosphate-
RT   dependent phosphofructo-1-kinase of Propionibacterium
RT   freudenreichii.";
RL   Biochemistry 31:4815-4821(1992).
CC   -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
CC       phosphate + D-fructose 1,6-bisphosphate.
CC   -!- ENZYME REGULATION: Non-allosteric.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. PFP
CC       subfamily.
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DR   EMBL; M67447; AAA25675.1; -; Genomic_DNA.
DR   PIR; A41169; A41169.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphot...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   InterPro; IPR000023; Ppfruckinase.
DR   InterPro; IPR011405; PPi-PFK_SMc01852.
DR   PANTHER; PTHR13697; Ppfruckinase; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   ProDom; PD000707; Ppfruckinase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    404       Pyrophosphate--fructose 6-phosphate 1-
FT                                phosphotransferase.
FT                                /FTId=PRO_0000112013.
FT   NP_BIND      22     26       ATP (By similarity).
FT   NP_BIND     121    126       Pyrophosphate (Potential).
FT   NP_BIND     179    183       ATP (By similarity).
FT   NP_BIND     196    232       ATP (By similarity).
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING     326    326       Substrate (By similarity).
SQ   SEQUENCE   404 AA;  43246 MW;  2676CD4ADE0D8A55 CRC64;
     MVKKVALLTA GGFAPCLSSA IAELIKRYTE VSPETTLIGY RYGYEGLLKG DSLEFSPAVR
     AHYDRLFSFG GSPIGNSRVK LTNVKDLVAR GLVASGDDPL KVAADQLIAD GVDVLHTIGG
     DDTNTTAADL AAYLAQHDYP LTVVGLPKTI DNDIVPIRQS LGAWTAADEG ARFAANVIAE
     HNAAPRELII HEIMGRNCGY LAAETSRRYV AWLDAQQWLP EAGLDRRGWD IHALYVPEAT
     IDLDAEAERL RTVMDEVGSV NIFISEGAGV PDIVAQMQAT GQEVPTDAFG HVQLDKINPG
     AWFAKQFAER IGAGKTMVQK SGYFSRSAKS NAQDLELIAA TATMAVDAAL AGTPGVVGQD
     EEAGDKLSVI DFKRIAGHKP FDITLDWYTQ LLARIGQPAP IAAA
//