ID   A0A3N2DLH2_9ENTR        Unreviewed;       320 AA.
AC   A0A3N2DLH2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   11-DEC-2019, entry version 6.
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 elegans.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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_00339,
CC       ECO:0000256|SAAS:SAAS01078966}.
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_00339, ECO:0000256|SAAS:SAAS01116210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00339,
CC         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) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS01228968}.
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: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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, 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, ECO:0000256|SAAS:SAAS00436062,
KW   ECO:0000313|EMBL:ROS00631.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, 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
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NP_BIND         73..74
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   NP_BIND         103..106
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          22..26
FT                   /note="Allosteric activator ADP binding; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          55..60
FT                   /note="Allosteric activator ADP binding; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          126..128
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          170..172
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          186..188
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          214..216
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          250..253
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   METAL           104
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         12
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         155
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         163
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         212
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         223
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         244
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="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
//