ID   B7WS18_COMTK            Unreviewed;       351 AA.
AC   B7WS18;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
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
RT   alkylbenzenesulfonate by defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01976, ECO:0000256|SAAS:SAAS00609123};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000256|SAAS:SAAS00358399}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
CC       ECO:0000256|SAAS:SAAS00551378}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}.
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; 31563855; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
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: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   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   Complete proteome {ECO:0000313|Proteomes:UP000003039};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041050};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041074};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041044, ECO:0000313|EMBL:EED69072.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041077};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041029};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041058, ECO:0000313|EMBL:EED69072.1}.
FT   DOMAIN        2    299       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND     105    108       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      128    130       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      172    174       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      274    277       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    130    130       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       106    106       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      10     10       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     165    165       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     224    224       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     268    268       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        107    107       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {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
//