ID G0HPK3_THES4 Unreviewed; 459 AA.
AC G0HPK3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ADP-specific phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00561};
DE EC=2.7.1.146 {ECO:0000256|HAMAP-Rule:MF_00561};
DE AltName: Full=ADP-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00561};
DE Short=ADP-Pfk {ECO:0000256|HAMAP-Rule:MF_00561};
GN Name=pfkC {ECO:0000256|HAMAP-Rule:MF_00561};
GN OrderedLocusNames=GQS_10400 {ECO:0000313|EMBL:AEK73973.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73973.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73973.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00561};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00561};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000256|HAMAP-
CC Rule:MF_00561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00561}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000256|HAMAP-Rule:MF_00561}.
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; CP002920; AEK73973.1; -; Genomic_DNA.
DR RefSeq; WP_014013655.1; NC_015865.1.
DR AlphaFoldDB; G0HPK3; -.
DR STRING; 1042877.GQS_10400; -.
DR GeneID; 11016764; -.
DR KEGG; the:GQS_10400; -.
DR PATRIC; fig|1042877.9.peg.2032; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OrthoDB; 85200at2157; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000874; 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; 3.30.1110.20; -; 1.
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 NCBIfam; TIGR02045; P_fruct_ADP; 1.
DR PANTHER; PTHR21208; ADP-DEPENDENT GLUCOKINASE; 1.
DR PANTHER; PTHR21208:SF1; ADP-DEPENDENT GLUCOKINASE; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00561};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00561};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00561};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00561};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00561}.
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
SQ SEQUENCE 459 AA; 52381 MW; 231161F988609B89 CRC64;
MGLLDEARKL SVYTAYNTNV DAITFLKGDI VQRLIDEFGA EAVRKRMDDY PREINEPLDF
VARLVHALKT GKPMAVPLVN EELHAWFDSH FKYDVERMGG QAGIIANLLA NLDFKRVLVY
TPHLARKQAK MFMDRPNLAY PVVEDGRLAF KHPREAYREG DPIKVNRIFE FRAGTTFRLG
NETIQVPFSG RFIVSARFES IRIYTDPELK PFLPEIGLQV DGAILSGYQG IKLRYSDGKD
ANHYLREAKK DILLLKREKD VKVHLEFASI QNRELRKKVI YNLFPLVDSV GMDEAEIAHV
LNALGYSKLS DRIFTYNRIE DTVLGGKILI DEMNLEVLQI HTIYYIMYIT HSDNPLSEDE
LRSSLELATT LAAARASLGE IRSPEDFKVG TSVPYNERGE YVKLRFEEAK RRLRTREYKV
VIIPTRLVRN PVSTVGLGDT ISAGAFTSYL AMLRKKGAL
//
