PFKA_TREPA
ID PFKA_TREPA Reviewed; 461 AA.
AC O83146;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01981};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01981}; Synonyms=pfk;
GN OrderedLocusNames=TP_0108; ORFNames=TPANIC_0108;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=24058545; DOI=10.1371/journal.pone.0074319;
RA Petrosova H., Pospisilova P., Strouhal M., Cejkova D., Zobanikova M.,
RA Mikalova L., Sodergren E., Weinstock G.M., Smajs D.;
RT "Resequencing of Treponema pallidum ssp. pallidum strains Nichols and SS14:
RT correction of sequencing errors resulted in increased separation of
RT syphilis treponeme subclusters.";
RL PLoS ONE 8:E74319-E74319(2013).
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_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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01981};
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_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01981}.
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DR EMBL; AE000520; AAC26556.1; -; Genomic_DNA.
DR EMBL; CP004010; AGN75327.1; -; Genomic_DNA.
DR PIR; A71366; A71366.
DR RefSeq; WP_010881557.1; NC_021490.2.
DR AlphaFoldDB; O83146; -.
DR SMR; O83146; -.
DR STRING; 243276.TPANIC_0108; -.
DR EnsemblBacteria; AAC26556; AAC26556; TP_0108.
DR EnsemblBacteria; AGN75327; AGN75327; TPANIC_0108.
DR GeneID; 57878648; -.
DR KEGG; tpa:TP_0108; -.
DR KEGG; tpw:TPANIC_0108; -.
DR PATRIC; fig|243276.9.peg.109; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_7_4_12; -.
DR OMA; KFAVICV; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000811; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 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; Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429713"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 156..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 182..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 380..383
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT SITE 184
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
SQ SEQUENCE 461 AA; 50162 MW; 6A902B8678CC8A54 CRC64;
MAHLPKEYDF SIESLGESKI PSPIYLSHTL GDFIPNYVSD NEYISHELSA RLGETVGPFT
HKNLMERAGP RQKIFFNPHH VHAGIVTCGG LCPGLNDVIR AIVRCLWGRY GVKRISGIRF
GYKGLLPDYN FDILPLTPEV IDNCHKTGGS LLGTSRGGGN RVVDIVDGIE RLNLHILFII
GGDGSQKGAK EIADEIKHRN LKISIIGIPK TVDNDISFVQ KSFGFDTAIV KATEAVAAAH
MEARSQINGI GLVKLMGRES GFIATYTAIA SHETNFVLIP EVSFDLDGPN GLLAHLEKRI
ALRKHAVLVV AEGAGQDLMV NADGVPSGDS QGGSLRVSSG TDASGNKRLA DIGLFLKEKI
GVYFKEKRIH INLKYIDPSY LIRSAVAAPI DSIYCERLGN NAVHAAMCGK TKMIIGLVHN
KFVHLPIDVV VCQRKHVNPE GSLWRDALDA TGQPIVMKNI I
