ID   Q75FU3_LEPIC            Unreviewed;       431 AA.
AC   Q75FU3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01981};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01981};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01981};
GN   Name=pfp {ECO:0000313|EMBL:AAS72117.1};
GN   Synonyms=pfkA {ECO:0000256|HAMAP-Rule:MF_01981};
GN   OrderedLocusNames=LIC_20088 {ECO:0000313|EMBL:AAS72117.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS72117.1, ECO:0000313|Proteomes:UP000007037};
RN   [1] {ECO:0000313|EMBL:AAS72117.1, ECO:0000313|Proteomes:UP000007037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS72117.1,
RC   ECO:0000313|Proteomes:UP000007037};
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA   Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA   De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA   Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA   Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(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_01981}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC         Rule:MF_01981};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_01981};
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_01981}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC       sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01981}.
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DR   EMBL; AE016824; AAS72117.1; -; Genomic_DNA.
DR   RefSeq; WP_000448293.1; NC_005824.1.
DR   AlphaFoldDB; Q75FU3; -.
DR   SMR; Q75FU3; -.
DR   GeneID; 61141284; -.
DR   KEGG; lic:LIC_20088; -.
DR   HOGENOM; CLU_020655_7_4_12; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000007037; Chromosome II.
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   Gene3D; 3.40.50.450; -; 1.
DR   HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR   PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01981};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01981};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01981};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01981}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01981}.
FT   DOMAIN          70..374
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         143..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         168..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         197..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         242..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   BINDING         350..353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT   SITE            170
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ   SEQUENCE   431 AA;  47758 MW;  DB7E31AECA344181 CRC64;
     METKIQNFGE CSIPSPADYE YYTSDTSRLI FRTVFQSKED WNSYVQEGPD FFEQAGPREK
     IYFNPQEVTA GIVTCGGLCP GINDVIRGIV MELYYRYGVS RILGFPYGYQ GLVKRYSHQP
     IELTPEKVAH IVDEGGSMLS SSRGNQSPEE MVDSLSFYGV KILFCIGGDG TLRGARTIVD
     EIAKRKEKIS VVGIPKTIDN DINYVQKTFG FSTAFSKAME AVECAHVEAK GAPNGIGLVK
     LMGRHSGFIA VNAALASRNV NYCLIPEVDF DLFGNEAFLD DLKKRIQKKG HAVIIVAEGA
     GQKFFDSTEE RDSSGNLKLK DIGLFLKDTM TEFFKKENIP VNIKYIDPSY IIRSIPANAE
     DSVFCGFLAQ NAVHAGMAGK TDMVVGMWNN VFTHLPISVA IQERKVLQPD RSTLWRSLLA
     STGQPAHMLA K
//