ID   K6PF_CORGL              Reviewed;         346 AA.
AC   Q8NR14;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=6-phosphofructokinase;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
GN   Name=pfkA; OrderedLocusNames=Cgl1250, cg1409;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000036; BAB98643.1; -; Genomic_DNA.
DR   EMBL; BX927151; CAF19953.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_600473.1; -.
DR   RefSeq; YP_225539.1; -.
DR   HSSP; P00512; 3PFK.
DR   World-2DPAGE; 0001:Q8NR14; -.
DR   PRIDE; Q8NR14; -.
DR   GeneID; 1019232; -.
DR   GeneID; 3344017; -.
DR   GenomeReviews; BA000036_GR; Cgl1250.
DR   GenomeReviews; BX927147_GR; cg1409.
DR   KEGG; cgb:cg1409; -.
DR   KEGG; cgl:NCgl1202; -.
DR   HOGENOM; Q8NR14; -.
DR   OMA; Q8NR14; ESHHRIM.
DR   BioCyc; CGLU196627-1:CG1409-MON; -.
DR   BRENDA; 2.7.1.11; 812.
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; IPR012829; PFK.
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; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    346       6-phosphofructokinase.
FT                                /FTId=PRO_0000111948.
FT   NP_BIND      23     27       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   BINDING     166    166       Substrate (By similarity).
FT   BINDING     270    270       Substrate (By similarity).
FT   BINDING     276    276       Substrate (By similarity).
FT   BINDING     279    279       Substrate (By similarity).
SQ   SEQUENCE   346 AA;  37464 MW;  96713869752962B0 CRC64;
     MEDMRIATLT SGGDCPGLNA VIRGIVRTAS NEFGSTVVGY QDGWEGLLGD RRVQLYDDED
     IDRILLRGGT ILGTGRLHPD KFKAGIDQIK ANLEDAGIDA LIPIGGEGTL KGAKWLSDNG
     IPVVGVPKTI DNDVNGTDFT FGFDTAVAVA TDAVDRLHTT AESHNRVMIV EVMGRHVGWI
     ALHAGMAGGA HYTVIPEVPF DIAEICKAME RRFQMGEKYG IIVVAEGALP REGTMELREG
     HIDQFGHKTF TGIGQQIADE IHVRLGHDVR TTVLGHIQRG GTPTAFDRVL ATRYGVRAAR
     ACHEGSFDKV VALKGESIEM ITFEEAVGTL KEVPFERWVT AQAMFG
//