ID   K6PF2_BACTN             Reviewed;         326 AA.
AC   Q8A624;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=6-phosphofructokinase 2;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphofructokinase 2;
DE   AltName: Full=Phosphohexokinase 2;
GN   Name=pfkA2; OrderedLocusNames=BT_2062;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO77169.1; -; Genomic_DNA.
DR   RefSeq; NP_810975.1; -.
DR   HSSP; P00512; 3PFK.
DR   GeneID; 1071883; -.
DR   GenomeReviews; AE015928_GR; BT_2062.
DR   KEGG; bth:BT_2062; -.
DR   NMPDR; fig|226186.1.peg.2062; -.
DR   HOGENOM; Q8A624; -.
DR   OMA; Q8A624; DTCLNTV.
DR   BioCyc; BTHE226186:BT_2062-MON; -.
DR   BRENDA; 2.7.1.11; 21018.
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   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   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    326       6-phosphofructokinase 2.
FT                                /FTId=PRO_0000111938.
FT   NP_BIND      24     28       ATP (By similarity).
FT   NP_BIND     158    162       ATP (By similarity).
FT   NP_BIND     175    191       ATP (By similarity).
FT   ACT_SITE    131    131       Proton acceptor (By similarity).
FT   METAL       189    189       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       191    191       Magnesium (By similarity).
FT   BINDING     166    166       Substrate (By similarity).
FT   BINDING     250    250       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
SQ   SEQUENCE   326 AA;  35257 MW;  EEF46D4915E7A082 CRC64;
     MGTVKCIGIL TSGGDAPGMN AAIRAVTRAA IYNGLQVKGI YRGYKGLVTG EIKEFKSQNV
     SNIIQLGGTI LKTARCKEFT TPEGRQLAYD NMKREGIDAL VIIGGDGSLT GARIFAQEFD
     VPCIGLPGTI DNDLYGTDTT IGYDTALNTI LDAVDKIRDT ATSHERLFFV EVMGRDAGFL
     ALNGAIASGA EAAIIPEFST EVDQLEEFIK NGFRKSKNSS IVLVAESELT GGAMHYAERV
     KNEYPQYDVR VTILGHLQRG GSPTAHDRIL ASRLGAAAID AIMEDQRNVM IGIEHDEIVY
     VPFSKAIKND KPVKRDLVNV LKELSI
//