ID   A0A3N2DLH2_9ENTR        Unreviewed;       320 AA.
AC   A0A3N2DLH2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   03-JUL-2019, entry version 4.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339};
GN   ORFNames=EC848_4567 {ECO:0000313|EMBL:ROS00631.1};
OS   Enterobacter sp. BIGb0359.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=2485133 {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546};
RN   [1] {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIGb0359 {ECO:0000313|EMBL:ROS00631.1,
RC   ECO:0000313|Proteomes:UP000281546};
RA   Samuel B.;
RT   "Genomic analyses of the natural microbiome of Caenorhabditis
RT   elegans.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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_00339,
CC       ECO:0000256|SAAS:SAAS01078966}.
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_00339,
CC         ECO:0000256|SAAS:SAAS01116210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00339, ECO:0000256|SAAS:SAAS00609123};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS01070487}.
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_00339, ECO:0000256|SAAS:SAAS00041065}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00557934}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00551378}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Prokaryotic clade
CC       "B1" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00541548}.
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:ROS00631.1}.
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DR   EMBL; RKHS01000009; ROS00631.1; -; Genomic_DNA.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000281546; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00763; Bacterial_PFK; 1.
DR   HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012828; PFKA_ATP_prok.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
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   TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00339};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00016785};
KW   Complete proteome {ECO:0000313|Proteomes:UP000281546};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436108};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436111};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:ROS00631.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436079};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436116};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00016719};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00436075}.
FT   DOMAIN        4    276       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND      73     74       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   NP_BIND     103    106       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION       22     26       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION       55     60       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      126    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      170    172       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      186    188       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      214    216       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      250    253       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    128    128       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   METAL       104    104       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      12     12       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     155    155       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     163    163       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     212    212       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   BINDING     244    244       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   320 AA;  35005 MW;  D15012D3F7858BD9 CRC64;
     MIKKIGVLTS GGDAPGMNAA IRGVVRSALA EGLEVFGIYD GYLGLYEDRM VQLDRYSVSD
     MINRGGTFLG SARFPEFRDD KVREIAIENM KKRGLDALVV IGGDGSYMGA KRLTEMGFPC
     IGLPGTIDND IKGTDYTIGY FTALGTVVEA IDRLRDTSSS HQRISIVEVM GRYCGDLTLA
     AAIAGGCEFV VVPEVEFSRE DLVAEIKAGI AKGKKHAIVA ITEHICDVDE LARFIETETK
     RETRSTVLGH IQRGGSPVPY DRILASRMGA YAIELLQQGY GGRCVGIQNE KLVHHDIIDA
     IENMKRPFKG DWLDCAKKLY
//