ID   B7WS18_COMTK            Unreviewed;       351 AA.
AC   B7WS18;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   02-JUN-2021, entry version 65.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976};
GN   ORFNames=CtesDRAFT_PD4020 {ECO:0000313|EMBL:EED69072.1};
OS   Comamonas testosteroni (strain DSM 14576 / 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=DSM 14576 / KF-1 {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 alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC       first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC       phosphoryl donor instead of ATP like common ATP-dependent
CC       phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC       and can thus function both in glycolysis and gluconeogenesis.
CC       Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC       PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC       {ECO:0000256|ARBA:ARBA00003138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01976};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC         Evidence={ECO:0000256|ARBA:ARBA00000628};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EED69072.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAUJ02000001; EED69072.1; -; Genomic_DNA.
DR   RefSeq; WP_003057959.1; NZ_AAUJ02000001.1.
DR   STRING; 399795.CtesDRAFT_PD4020; -.
DR   EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020.
DR   GeneID; 60801090; -.
DR   eggNOG; COG0205; 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-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
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   InterPro; IPR035966; PKF_sf.
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|HAMAP-Rule:MF_01976};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01976};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01976};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01976};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01976};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01976}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01976}.
FT   DOMAIN          2..299
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NP_BIND         105..108
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          128..130
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          172..174
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          274..277
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   METAL           106
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         10
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         165
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         224
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         268
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   SITE            107
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
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
//