K6PF_THEZI
ID K6PF_THEZI Reviewed; 461 AA.
AC Q9HH12;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
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}; Synonyms=pfk;
OS Thermococcus zilligii.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=54076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=AN1;
RX PubMed=11342216; DOI=10.1016/s0167-4781(00)00301-8;
RA Ronimus R.S., de Heus E., Morgan H.W.;
RT "Sequencing, expression, characterization and phylogeny of the ADP-
RT dependent phosphofructokinase from the hyperthermophilic, euryarchaeal
RT Thermococcus zilligii.";
RL Biochim. Biophys. Acta 1517:384-391(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor.
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.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000255|HAMAP-Rule:MF_00561}.
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DR EMBL; AY005811; AAF97356.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HH12; -.
DR SMR; Q9HH12; -.
DR BRENDA; 2.7.1.146; 6306.
DR UniPathway; UPA00109; -.
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; Transferase.
FT CHAIN 1..461
FT /note="ADP-specific phosphofructokinase"
FT /id="PRO_0000184770"
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; 52758 MW; E325A326F62D6298 CRC64;
MVRELLEKAR GLSIYTAYNT NVDAIVYLNG ETVQRLIDEF GADAVRKRME DYPREINEPL
DFVARLVHAL KTGKPMAVPL VNEELHTWFD SHFRYDVERM GGQAGIIANL LSNLDFREVI
VYTPHLAKRQ AEMFVRKPNL FYPVVEGGRL VLKHPWEAYR EGDPVKVNRI FEFRAGTAFK
LGDERIVVPF SGRFIVSARF ESIRIYTEPG LRPFLPEIGE RVDGAILSGY QGINLRYSDG
KDANYYLRKA KEDIMLLKRE KDLKVHLEFA SIQSRELRKK VIYNLFPLAD SVGMDEAEIA
YVLSALGYDE LADRIFTYNR IEDTVLGGKI LLDEMNLDVL QIHTIYYIMY ITHADNPLSE
EELRRSLELA TTLAASRASL GDITSPDQIE IGLRVPYNER GEYVKLRFEE AKRKLRTKEY
KLVIIPTRLV QNPVSTVGLG DTISTGAFAS YLAMLKEKGE L
