ID   B7WS18_COMTE            Unreviewed;       351 AA.
AC   B7WS18;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   09-DEC-2015, entry version 41.
DE   SubName: Full=6-phosphofructokinase {ECO:0000313|EMBL:EED69072.1};
DE            EC=2.7.1.11 {ECO:0000313|EMBL:EED69072.1};
GN   ORFNames=CtesDRAFT_PD4020 {ECO:0000313|EMBL:EED69072.1};
OS   Comamonas testosteroni KF-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=399795 {ECO:0000313|EMBL:EED69072.1, ECO:0000313|Proteomes:UP000003039};
RN   [1] {ECO:0000313|EMBL:EED69072.1, ECO:0000313|Proteomes:UP000003039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF-1 {ECO:0000313|EMBL:EED69072.1,
RC   ECO:0000313|Proteomes:UP000003039};
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).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|SAAS:SAAS00358399}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00366550}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EED69072.1}.
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DR   EMBL; AAUJ02000001; EED69072.1; -; Genomic_DNA.
DR   RefSeq; WP_003057959.1; NZ_AAUJ02000001.1.
DR   ProteinModelPortal; B7WS18; -.
DR   STRING; 399795.CtesDRAFT_PD4020; -.
DR   EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020.
DR   GeneID; 8561475; -.
DR   PATRIC; 29059527; VBIComTes39478_3969.
DR   eggNOG; COG0205; LUCA.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000003039; Unassembled WGS sequence.
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   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   ATP-binding {ECO:0000256|RuleBase:RU004092};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003039};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00041050};
KW   Glycolysis {ECO:0000256|SAAS:SAAS00041074};
KW   Kinase {ECO:0000256|RuleBase:RU004092, ECO:0000256|SAAS:SAAS00041044,
KW   ECO:0000313|EMBL:EED69072.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00041077};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00041029};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004092};
KW   Transferase {ECO:0000256|RuleBase:RU004092,
KW   ECO:0000256|SAAS:SAAS00041058, ECO:0000313|EMBL:EED69072.1}.
FT   DOMAIN        2    299       PFK. {ECO:0000259|Pfam:PF00365}.
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
//