ID   B7WS18_COMTE            Unreviewed;       351 AA.
AC   B7WS18;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JUN-2014, entry version 26.
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   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Subject to allosteric activation by ADP and
CC       other diphosphonucleosides, and inhibition by phosphoenolpyruvate
CC       (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; AAUJ02000001; EED69072.1; -; Genomic_DNA.
DR   ProteinModelPortal; B7WS18; -.
DR   EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020.
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:UniProtKB-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:glycolytic process; IEA:UniProtKB-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; SSF53784; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT   NP_BIND     105    108       ATP (By similarity){EA11}.
FT   REGION      128    130       Substrate binding (By similarity).
FT   REGION      172    174       Substrate binding (By similarity).
FT   REGION      274    277       Substrate binding (By similarity).
FT   ACT_SITE    130    130       Proton acceptor (By similarity){EA11}.
FT   METAL       106    106       Magnesium; catalytic (By
FT                                similarity){EA11}.
FT   BINDING      10     10       ATP; via amide nitrogen (By
FT                                similarity){EA11}.
FT   BINDING     165    165       Substrate; shared with dimeric partner
FT                                (By similarity){EA11}.
FT   BINDING     224    224       Substrate (By similarity){EA11}.
FT   BINDING     268    268       Substrate; shared with dimeric partner
FT                                (By similarity){EA11}.
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
//