K6PF_PYRFU
ID K6PF_PYRFU Reviewed; 454 AA.
AC Q9V2Z7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ADP-specific phosphofructokinase;
DE EC=2.7.1.146;
DE AltName: Full=ADP-dependent phosphofructokinase;
DE Short=ADP-Pfk;
GN Name=pfkC; Synonyms=pfkA; OrderedLocusNames=PF1784;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10409652; DOI=10.1074/jbc.274.30.21023;
RA Tuininga J.E., Verhees C.H., van der Oost J., Kengen S.W.M., Stams A.J.M.,
RA de Vos W.M.;
RT "Molecular and biochemical characterization of the ADP-dependent
RT phosphofructokinase from the hyperthermophilic archaeon Pyrococcus
RT furiosus.";
RL J. Biol. Chem. 274:21023-21028(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor. As a
CC phosphoryl group donor, ADP can be replaced by GDP, ATP, and GTP to a
CC limited extent.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + beta-D-fructose 6-phosphate = AMP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:20105, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=2.7.1.146;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by AMP and ATP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for fructose 6-phosphate;
CC KM=0.11 mM for ADP;
CC Vmax=194 umol/min/mg enzyme with fructose 6-phosphate as substrate;
CC Vmax=150 umol/min/mg enzyme with ADP as substrate;
CC Note=The kinetic parameters were measured at 50 degrees Celsius.;
CC pH dependence:
CC Optimum pH is 6.5.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000305}.
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DR EMBL; AF127909; AAD48400.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81908.1; -; Genomic_DNA.
DR RefSeq; WP_011012925.1; NC_018092.1.
DR AlphaFoldDB; Q9V2Z7; -.
DR SMR; Q9V2Z7; -.
DR STRING; 186497.PF1784; -.
DR PRIDE; Q9V2Z7; -.
DR EnsemblBacteria; AAL81908; AAL81908; PF1784.
DR GeneID; 41713602; -.
DR KEGG; pfu:PF1784; -.
DR PATRIC; fig|186497.12.peg.1855; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OMA; NRIFEFR; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; Q9V2Z7; -.
DR BioCyc; MetaCyc:MON-11808; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043844; F:ADP-specific phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008443; F:phosphofructokinase activity; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00561; ADP_PFKinase; 1.
DR InterPro; IPR007666; ADP_PFK/GK.
DR InterPro; IPR015990; ADP_PFK/GK_arc.
DR InterPro; IPR011790; ADP_PFK_arc.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02045; P_fruct_ADP; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="ADP-specific phosphofructokinase"
FT /id="PRO_0000184766"
FT DOMAIN 1..452
FT /note="ADPK"
FT ACT_SITE 436
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 52337 MW; 390F32584ECD0DC8 CRC64;
MIDEVRELGI YTAYNANVDA IVNLNAEIIQ RLIEEFGPDK IKRRLEEYPR EINEPLDFVA
RLVHALKTGK PMAVPLVNEE LHQWFDKTFK YDTERIGGQA GIIANILVGL KVKKVIAYTP
FLPKRLAELF KEGILYPVVE EDKLVLKPIQ SAYREGDPLK VNRIFEFRKG TRFKLGDEVI
EVPHSGRFIV SSRFESISRI ETKDELRKFL PEIGEMVDGA ILSGYQGIRL QYSDGKDANY
YLRRAKEDIR LLKKNKDIKI HVEFASIQDR RLRKKVVNNI FPMVDSVGMD EAEIAYILSV
LGYSDLADRI FMYNRIEDAI LGGMIILDEL NFEILQVHTI YYLMYITHRD NPLSEEELMR
SLDFGTILAA TRASLGDIND PRDVKVGMSV PYNERSEYIK LRFEEAKRKL RLKEYKVVIV
PTRLVPNPVS TVGLGDTIST GTFLSYLSLL RRHQ
