ID   B7WS18_COMTE            Unreviewed;       351 AA.
AC   B7WS18;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   31-OCT-2012, entry version 20.
DE   RecName: Full=6-phosphofructokinase;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
GN   Name=pfkA; ORFNames=CtesDRAFT_PD4020;
OS   Comamonas testosteroni KF-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=399795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KF-1;
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear
RT   alkylbenzenesulfonate by defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KF-1;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Lowry S.,
RA   Sun H., Larimer F., Land M.L., Hauser L., Kjelleberg S., Cook A.,
RA   Knepper T.P., Fischer K., Schleheck D., Richardson P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family.
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DR   EMBL; AAUJ02000001; EED69072.1; -; Genomic_DNA.
DR   ProteinModelPortal; B7WS18; -.
DR   PATRIC; 29059527; VBIComTes39478_3969.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_00339; Phosphofructokinase; 1; -.
DR   InterPro; IPR012003; ATP_PFK_prok.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Ppfruckinase; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   NP_BIND      20     24       ATP (By similarity).
FT   NP_BIND     157    161       ATP (By similarity).
FT   NP_BIND     174    190       ATP (By similarity).
FT   ACT_SITE    130    130       Proton acceptor (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   BINDING     268    268       Substrate (By similarity).
FT   BINDING     274    274       Substrate (By similarity).
FT   BINDING     277    277       Substrate (By similarity).
SQ   SEQUENCE   351 AA;  37162 MW;  2055B26C6FCB5E9E CRC64;
     MRVGVLTGGG DCPGLNAVIR AVTKSLINHG QCEVLGIADG FEGLMDASPR VRALSWDEVS
     GILHIGGTIL GTSNSANPLR DAATLAQVGR NVKALALDVV VAIGGDGTMS LAHGLAQVGL
     QCVGVPKTID NDIANCERSF GFDTAVATVT ESLRRIESTA MSHHRVMIVE TMGRHAGWLA
     LESGIAGAAD IILLPEIDYD LQSIIKVCQE RERRQRYTII CIGEGAKESG QSLTVRERIA
     HSPDPVRLGG VGHVLRERLQ PHLQSEVRTT VLGHVQRGGD PTPFDRVLAT QFGHHAAQLV
     LGGQLGHMVT LQNGRIGSVA IADVANTQRT VPLDSPLLTM ARDIGICFGE A
//