ID   PFP_BORBU               Reviewed;         555 AA.
AC   P70826;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   27-MAR-2024, entry version 117.
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}; Synonyms=PFK2, pfpB;
GN   OrderedLocusNames=BB_0020;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HB19;
RX   PubMed=9766225; DOI=10.1016/s0923-2508(98)80299-4;
RA   Boursaux-Eude C., Margarita D., Belfaiza J., Old I.G., Saint-Girons I.;
RT   "Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the
RT   Lyme borreliosis agent.";
RL   Res. Microbiol. 149:235-245(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=10545221; DOI=10.1006/abbi.1999.1446;
RA   Deng Z., Roberts D., Wang X., Kemp R.G.;
RT   "Expression, characterization, and crystallization of the pyrophosphate-
RT   dependent phosphofructo-1-kinase of Borrelia burgdorferi.";
RL   Arch. Biochem. Biophys. 371:326-331(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-553.
RX   PubMed=12015149; DOI=10.1016/s0969-2126(02)00760-8;
RA   Moore S.A., Ronimus R.S., Roberson R.S., Morgan H.W.;
RT   "The structure of a pyrophosphate-dependent phosphofructokinase from the
RT   Lyme disease spirochete Borrelia burgdorferi.";
RL   Structure 10:659-671(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 1-553 IN COMPLEX WITH SUBSTRATE.
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA   Wang M., Grum-Tokars V.;
RT   "Crystal structure of a novel fructose 1,6-bisphosphate and AlF(3)
RT   containing pyrophosphate-dependent phosphofructo-1-kinase complex from
RT   Borrelia burgdorferi.";
RL   Submitted (NOV-2005) to the PDB data bank.
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:10545221}.
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:10545221};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-
CC         Rule:MF_01980};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000250|UniProtKB:Q9EZ02,
CC       ECO:0000255|HAMAP-Rule:MF_01980}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for diphosphate {ECO:0000269|PubMed:10545221};
CC         KM=109 uM for D-fructose 6-phosphate {ECO:0000269|PubMed:10545221};
CC       pH dependence:
CC         Optimum pH is 6.4-7.2. {ECO:0000269|PubMed:10545221};
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:10545221, ECO:0000269|Ref.5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796,
CC       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}.
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DR   EMBL; AJ224475; CAA11968.1; -; Genomic_DNA.
DR   EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; D70102; D70102.
DR   PDB; 1KZH; X-ray; 2.55 A; A/B=1-553.
DR   PDB; 2F48; X-ray; 2.11 A; A/B=1-553.
DR   PDBsum; 1KZH; -.
DR   PDBsum; 2F48; -.
DR   AlphaFoldDB; P70826; -.
DR   SMR; P70826; -.
DR   BioCyc; MetaCyc:MONOMER-21288; -.
DR   SABIO-RK; P70826; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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   CDD; cd00765; Pyrophosphate_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 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   NCBIfam; TIGR02477; PFKA_PPi; 1.
DR   PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..555
FT                   /note="Pyrophosphate--fructose 6-phosphate 1-
FT                   phosphotransferase"
FT                   /id="PRO_0000428943"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-
FT                   Rule:MF_01980"
FT   BINDING         82
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01980,
FT                   ECO:0000269|Ref.5"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|Ref.5"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-
FT                   Rule:MF_01980"
FT   BINDING         204..206
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                   ECO:0000269|Ref.5"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01980,
FT                   ECO:0000269|Ref.5"
FT   BINDING         251..253
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                   ECO:0000269|Ref.5"
FT   BINDING         312
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                   ECO:0000269|Ref.5"
FT   BINDING         428..431
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                   ECO:0000269|Ref.5"
FT   SITE            177
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                   ECO:0000305|PubMed:12015149"
FT   SITE            203
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,
FT                   ECO:0000305|PubMed:12015149"
FT   HELIX           5..10
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           42..48
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   TURN            49..54
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          74..82
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           87..101
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           127..133
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           152..164
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           176..191
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          197..204
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           220..241
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          245..250
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           257..266
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           274..279
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           284..300
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          306..311
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           319..334
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           336..339
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           344..354
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           357..364
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           368..379
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           394..410
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   TURN            411..413
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          421..427
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           428..431
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           437..455
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          460..466
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           472..474
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          476..481
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           482..485
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          486..491
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          494..499
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           509..523
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   STRAND          535..537
FT                   /evidence="ECO:0007829|PDB:1KZH"
FT   HELIX           539..542
FT                   /evidence="ECO:0007829|PDB:2F48"
FT   HELIX           547..552
FT                   /evidence="ECO:0007829|PDB:2F48"
SQ   SEQUENCE   555 AA;  62443 MW;  0FEAC1077DA6127F CRC64;
     MNTSLFKQER QKYIPKLPNI LKKDFNNISL VYGENTEAIQ DRQALKEFFK NTYGLPIISF
     TEGESSLSFS KALNIGIILS GGPAPGGHNV ISGVFDAIKK FNPNSKLFGF KGGPLGLLEN
     DKIELTESLI NSYRNTGGFD IVSSGRTKIE TEEHYNKALF VAKENNLNAI IIIGGDDSNT
     NAAILAEYFK KNGENIQVIG VPKTIDADLR NDHIEISFGF DSATKIYSEL IGNLCRDAMS
     TKKYWHFVKL MGRSASHVAL ECALKTHPNI CIVSEEVLAK KKTLSEIIDE MVSVILKRSL
     NGDNFGVVIV PEGLIEFIPE VKSLMLELCD IFDKNEGEFK GLNIEKMKEI FVAKLSDYMK
     GVYLSLPLFI QFELIKSILE RDPHGNFNVS RVPTEKLFIE MIQSRLNDMK KRGEYKGSFT
     PVDHFFGYEG RSAFPSNFDS DYCYSLGYNA VVLILNGLTG YMSCIKNLNL KPTDWIAGGV
     PLTMLMNMEE RYGEKKPVIK KALVDLEGRP FKEFVKNRDK WALNNLYLYP GPVQYFGSSE
     IVDEITETLK LELLK
//