ID   K6PF_BACCE              Reviewed;         319 AA.
AC   Q4MVY3; P83066;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=6-phosphofructokinase;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
GN   Name=pfkA; Synonyms=pfk; ORFNames=BCE_G9241_4679;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G9241;
RX   PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA   Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA   Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA   Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z.,
RA   Rilstone J., Peterson S.N., Weyant R.S., Galloway D.R., Read T.D.,
RA   Popovic T., Fraser C.M.;
RT   "Identification of anthrax toxin genes in a Bacillus cereus associated
RT   with an illness resembling inhalation anthrax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, AND INDUCTION.
RC   STRAIN=NCIMB 11796 / DSM 626;
RX   PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x;
RA   Browne N., Dowds B.C.A.;
RT   "Heat and salt stress in the food pathogen Bacillus cereus.";
RL   J. Appl. Microbiol. 91:1085-1094(2001).
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   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- INDUCTION: By salt stress.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family.
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DR   EMBL; AAEK01000003; EAL16121.1; -; Genomic_DNA.
DR   SMR; Q4MVY3; 1-319.
DR   BRENDA; 2.7.1.11; 604.
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:0000287; F:magnesium ion 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   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   HAMAP; MF_00339; -; 1.
DR   InterPro; IPR012003; ATP_PFK_prok.
DR   InterPro; IPR012828; PFKA_ATP.
DR   InterPro; IPR000023; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   ProDom; PD000707; Ppfruckinase; 1.
DR   TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Stress response; Transferase.
FT   CHAIN         1    319       6-phosphofructokinase.
FT                                /FTId=PRO_0000271249.
FT   NP_BIND      21     25       ATP (By similarity).
FT   NP_BIND     154    158       ATP (By similarity).
FT   NP_BIND     171    187       ATP (By similarity).
FT   ACT_SITE    127    127       Proton acceptor (By similarity).
FT   METAL       185    185       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       187    187       Magnesium (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   BINDING     243    243       Substrate (By similarity).
FT   BINDING     249    249       Substrate (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
SQ   SEQUENCE   319 AA;  34308 MW;  F655330A5044C628 CRC64;
     MKRIGVLTSG GDSPGMNAAI RAVVRKAIFH DIEVYGIYHG YAGLISGHIE KLELGSVGDI
     IHRGGTKLYT ARCPEFKDPE VRLKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEQGFPCV
     GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA
     GLADGAETIL IPEEEYDMED VIARLKRGSE RGKKHSIIVV AEGVGSAIDI GKHIEEATNF
     DTRVTVLGHV QRGGSPSAQD RVLASRLGAR AVELLIAGKG GRCVGIQDNK LVDHDIIEAL
     AQKHTIDKDM YQLSKELSI
//