PFP_BORBU
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 03-AUG-2022, entry version 112.
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; Spirochaetes; Spirochaetales; Borreliaceae; 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,
CC ECO:0000255|HAMAP-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:MON-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 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 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
