PFKA_SPITD
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 03-AUG-2022, entry version 60.
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; Spirochaetes; Spirochaetales; Spirochaetaceae; 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;
CC Evidence={ECO:0000255|HAMAP-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 STRING; 665571.STHERM_c00290; -.
DR PRIDE; E0RTD9; -.
DR EnsemblBacteria; ADN01005; ADN01005; STHERM_c00290.
DR KEGG; sta:STHERM_c00290; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_0_12; -.
DR OMA; TNRDNPF; -.
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; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 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
