PFP_TREPA
ID PFP_TREPA Reviewed; 573 AA.
AC O83553;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01980};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01980};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01980};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01980}; OrderedLocusNames=TP_0542;
GN ORFNames=TPANIC_0542;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=11164318; DOI=10.1111/j.1574-6968.2001.tb09479.x;
RA Roberson R.S., Ronimus R.S., Gephard S., Morgan H.W.;
RT "Biochemical characterization of an active pyrophosphate-dependent
RT phosphofructokinase from Treponema pallidum.";
RL FEMS Microbiol. Lett. 194:257-260(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|PubMed:11164318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:11164318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01980};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:11164318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.39 mM for phosphate {ECO:0000269|PubMed:11164318};
CC KM=0.042 mM for diphosphate {ECO:0000269|PubMed:11164318};
CC KM=0.529 mM for fructose 6-phosphate {ECO:0000269|PubMed:11164318};
CC KM=0.267 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:11164318};
CC Vmax=141 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:11164318};
CC Vmax=42.4 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:11164318};
CC pH dependence:
CC Optimum pH is 8.0 for both the forward and reverse reactions.
CC {ECO:0000269|PubMed:11164318};
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_01980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:11164318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01980}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01980}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000520; AAC65526.1; -; Genomic_DNA.
DR EMBL; CP004010; AGN75729.1; -; Genomic_DNA.
DR PIR; C71312; C71312.
DR RefSeq; WP_010881989.1; NC_021490.2.
DR AlphaFoldDB; O83553; -.
DR SMR; O83553; -.
DR IntAct; O83553; 3.
DR STRING; 243276.TPANIC_0542; -.
DR PRIDE; O83553; -.
DR EnsemblBacteria; AAC65526; AAC65526; TP_0542.
DR EnsemblBacteria; AGN75729; AGN75729; TPANIC_0542.
DR KEGG; tpa:TP_0542; -.
DR KEGG; tpw:TPANIC_0542; -.
DR PATRIC; fig|243276.9.peg.538; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_022288_0_1_12; -.
DR OMA; SAKKYWH; -.
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:InterPro.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
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_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..573
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429711"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 90
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 212..214
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 251..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 259..261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 320
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 434..437
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT SITE 185
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT SITE 211
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
SQ SEQUENCE 573 AA; 62427 MW; 3A9A95B01CBC134E CRC64;
MSISLLQQER HRYLPKVPDL LRGDFRRVCA RRGLSTTAVA DYDALRSLFA RTYGQPLVNF
VNASEKNEDS PMETAPEPRG LRVAIVLSGG QAPGGHNVIA GLFDGLKRWH ADSVLIGFLG
GPAGVLSGDH IEICADRVDA YRNTGGFDLI GSGRTKIESE SQFAAAAQTV TRMALDALVV
VGGDDSNTNA ALLAEHFVNS GISTKVIGVP KTIDGDLKNE AIETSFGFDT ATKTYSELIG
NIARDACSAR KYWHFIKLMG RSASHIALEC ALKTQPNVCL ISEEVAAQSL TLAQIVQSLC
DTIATRAQHG EHFGIVLVPE GLIEFIPEMK ALITELNEVM ARRAQEFEAL DTPDAQRVWI
EQALSASARA VFNALPAEIS TQLLADRDPH GNVQVSRIDT ERLLILQVTE RLAQMKQEGT
YTGVFSSIAH FFGYEGRCAF PSNFDADYCY TLGLTACLLA VHRFTGYVAS VRNLTSSVAE
WAVGGVPLTM LMNMERRHGS QKPVIKKALV DLEGMPFRVF SRRRASWALK TSYVYPGAVQ
YYGPPAVCDE PSVTIRLERP APAANSSFGH RSS
