K6PF_THEKO
ID K6PF_THEKO Reviewed; 461 AA.
AC Q5JD05;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ADP-specific phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00561};
DE EC=2.7.1.146 {ECO:0000255|HAMAP-Rule:MF_00561};
DE AltName: Full=ADP-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00561};
DE Short=ADP-Pfk {ECO:0000255|HAMAP-Rule:MF_00561};
GN Name=pfkC {ECO:0000255|HAMAP-Rule:MF_00561}; OrderedLocusNames=TK0376;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor.
CC {ECO:0000255|HAMAP-Rule:MF_00561}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00561};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00561};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00561}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000255|HAMAP-Rule:MF_00561}.
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DR EMBL; AP006878; BAD84565.1; -; Genomic_DNA.
DR RefSeq; WP_011249331.1; NC_006624.1.
DR AlphaFoldDB; Q5JD05; -.
DR SMR; Q5JD05; -.
DR STRING; 69014.TK0376; -.
DR EnsemblBacteria; BAD84565; BAD84565; TK0376.
DR GeneID; 3235316; -.
DR KEGG; tko:TK0376; -.
DR PATRIC; fig|69014.16.peg.373; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR InParanoid; Q5JD05; -.
DR OMA; NRIFEFR; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; Q5JD05; -.
DR BRENDA; 2.7.1.11; 5246.
DR BRENDA; 2.7.1.146; 5246.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000536; 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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="ADP-specific phosphofructokinase"
FT /id="PRO_0000184768"
FT DOMAIN 1..457
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
SQ SEQUENCE 461 AA; 52662 MW; 7C90AE49F3EC670F CRC64;
MVRELLEKAR GLSMFTAYNT NVDAIVYLNG ETVQRLIDEF GAEAVKRRME EYPREINEPL
DFVARLVHAL KTGKPMAVPL VNEELQAWFD SHFKYDVERM GGQAGIIANL LANLDFREVL
VYTPHLAKRQ AEMFVKKPNL FYPVVEGGKL VLKHPWEAYR ENDPVKVNRI FEFRAGTTFR
LGNETITVPF SGRFIVSARF ESIRIYTEPE LKPFLPEIGQ RVDGAILSGY QGIKLRYSDG
KDANYYLREA KKDILLLKRE KDVKVHLEFA SIQNRELRKK VIYNLFPLVD SVGMDEAEIA
YVLSALGYDK LAERIFTYNR IEDTVLGGKI LIDEMNLELL QIHTIYYIMY IAHANNPLSE
AELRQSLELA TTLAASRASL GDIASPDQIS VGMNVPYNER GEYVKLRFEE AKRRLRTKEY
KLVIIPTRLV QNPVSTVGLG DTISTGAFTS YLAMLKEKGE L
