ID   PFKA_SPITD              Reviewed;         366 AA.
AC   E0RTD9; Q9AG65;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfkA3;
GN   OrderedLocusNames=STHERM_c00290;
OS   Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=665571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1;
RX   PubMed=20935097; DOI=10.1128/jb.01023-10;
RA   Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA   Daniel R., Liebl W.;
RT   "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT   Spirochaeta thermophila DSM 6192.";
RL   J. Bacteriol. 192:6492-6493(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-145.
RX   PubMed=11382227; DOI=10.1007/s002030100265;
RA   Ronimus R., de Heus E., Ruckert A., Morgan H.;
RT   "Sequencing, high-level expression and phylogeny of the pyrophosphate-
RT   dependent phosphofructokinase from the thermophilic spirochete Spirochaeta
RT   thermophila.";
RL   Arch. Microbiol. 175:308-312(2001).
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:0000255|HAMAP-Rule:MF_01976}.
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:0000255|HAMAP-
CC         Rule:MF_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01976};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01976}.
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DR   EMBL; CP001698; ADN01005.1; -; Genomic_DNA.
DR   EMBL; AF342985; AAK16737.1; -; Genomic_DNA.
DR   RefSeq; WP_013312846.1; NC_014484.1.
DR   AlphaFoldDB; E0RTD9; -.
DR   SMR; E0RTD9; -.
DR   PaxDb; 665571-STHERM_c00290; -.
DR   KEGG; sta:STHERM_c00290; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_0_0_12; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001296; Chromosome.
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   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   InterPro; IPR035966; PKF_sf.
DR   PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..366
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000429709"
FT   REGION          74..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         78..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         118..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         141..143
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         185..187
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         288..291
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   SITE            120
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ   SEQUENCE   366 AA;  39845 MW;  7D2B4DE9F78372AB CRC64;
     MKRPATRTFG ILTSGGDCPG LNAAIRGVTK AAYWRYGMSI IGISHGYRGL IEGDARLLHP
     RDFDGILTRG GTILGTSREK PFKPDPGEKD SEAGSRKVEA IIENYHKLHL DCLVVLGGNG
     THKTAYLLQQ AGLNVIGLPK TIDNDIWGTD VTFGFHSAVD IATEAIDRLH STAHAHNRVM
     VIEVMGHKAG WLALYAGIAG GGDIILIPEI PYDLAHIVHH LQTRQQRGKE FSIVVVAEGA
     LSREESLMSK EERKKRRKKN RFPTKGYEVA HLIQEATGME TRVTVLGYLQ RGGTPSPYDR
     LLATRFGTAA AELLYRGDYG KMVALRDGEV VAIPLGEVAE KLKTVPPDHP LIDTARAVGT
     CFGDGV
//