ID   K6PF_PYRAB              Reviewed;         451 AA.
AC   Q9V1A6; G8ZGN1;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=PYRAB05210;
GN   ORFNames=PAB2013;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49443.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69910.1; -; Genomic_DNA.
DR   PIR; D75170; D75170.
DR   RefSeq; WP_010867645.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1A6; -.
DR   SMR; Q9V1A6; -.
DR   STRING; 272844.PAB2013; -.
DR   EnsemblBacteria; CAB49443; CAB49443; PAB2013.
DR   GeneID; 1495423; -.
DR   KEGG; pab:PAB2013; -.
DR   PATRIC; fig|272844.11.peg.556; -.
DR   eggNOG; arCOG03370; Archaea.
DR   HOGENOM; CLU_046643_0_0_2; -.
DR   OMA; NRIFEFR; -.
DR   OrthoDB; 15153at2157; -.
DR   PhylomeDB; Q9V1A6; -.
DR   UniPathway; UPA00109; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..451
FT                   /note="ADP-specific phosphofructokinase"
FT                   /id="PRO_0000184765"
FT   DOMAIN          1..450
FT                   /note="ADPK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT   ACT_SITE        434
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT   BINDING         434
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
SQ   SEQUENCE   451 AA;  51465 MW;  B65ED022B7D1096F CRC64;
     MSVPQDVSIF TAYNANVDAI TKLNGETIQK LINEFGEKEI AERIEEYPRE IREPIDFVAR
     LIHALRLGKP TAVPLVDESL NSWFDEKFEY ELERLGGQAG IIANVLAGLG IKKVIAYTPF
     LPKRLADLFK EGVLYPTVEN GELKLKPIRE AYRDEDPLKI NRIFEFRKGT KFKFLGESVE
     VPASGRFIVS ARFESISKIE TKEELRPFLD DIGKEVDGAI FSGYQGLRLK YSDGKDANYY
     LRRAKEDIIS LKEEDVKVHV ELASIQDRKL RKKVITNILP IADSVGIDEA EIAQLLSVLG
     YRDLADRIFT YNRLEDSILG GMIILDELNF EILQVHTIYY LMYITHRDNP LSEEELMKSL
     EFGTTLAAAR ASLGDINRPE DYEIGLKVPF NERSEYVKLR FEEAKTKLRM REYKVVVIPT
     RLVPNPVLTV GLGDTISAGA FITYVNYLKR H