K6PF_PYRHO
ID K6PF_PYRHO Reviewed; 450 AA.
AC O59355;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=PH1645;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30757.1; -; Genomic_DNA.
DR PIR; E71044; E71044.
DR RefSeq; WP_010885713.1; NC_000961.1.
DR PDB; 1U2X; X-ray; 2.00 A; A/B=1-450.
DR PDB; 3DRW; X-ray; 1.90 A; A/B=1-450.
DR PDBsum; 1U2X; -.
DR PDBsum; 3DRW; -.
DR AlphaFoldDB; O59355; -.
DR SMR; O59355; -.
DR IntAct; O59355; 1.
DR MINT; O59355; -.
DR STRING; 70601.3258074; -.
DR EnsemblBacteria; BAA30757; BAA30757; BAA30757.
DR GeneID; 1442494; -.
DR KEGG; pho:PH1645; -.
DR eggNOG; arCOG03370; Archaea.
DR OMA; NRIFEFR; -.
DR OrthoDB; 15153at2157; -.
DR BRENDA; 2.7.1.146; 5244.
DR UniPathway; UPA00109; -.
DR EvolutionaryTrace; O59355; -.
DR Proteomes; UP000000752; 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 3D-structure; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..450
FT /note="ADP-specific phosphofructokinase"
FT /id="PRO_0000184767"
FT DOMAIN 1..449
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 132..146
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3DRW"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 352..372
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:3DRW"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:3DRW"
FT HELIX 431..447
FT /evidence="ECO:0007829|PDB:3DRW"
SQ SEQUENCE 450 AA; 51753 MW; EC3B0836AA9314FE CRC64;
MIPEHLSIYT AYNANIDAIV KLNQETIQNL INAFDPDEVK RRIEEYPREI NEPIDFVARL
VHTLKLGKPA AVPLVNEKMN EWFDKTFRYE EERLGGQAGI IANTLAGLKI RKVIAYTPFL
PKRLAELFKK GVLYPVVENG ELQFKPIQEA YREGDPLKIN RIFEFRKGLK FKLGDETIEI
PNSGRFIVSA RFESISRIET REDIKPFLGE IGKEVDGAIF SGYQGLRTKY SDGKDANYYL
RRAKEDIIEF KEKDVKIHVE FASVQDRKLR KKIITNILPF VDSVGIDEAE IAQILSVLGY
RELADRIFTY NRLEDSILGG MIILDELNFE ILQVHTTYYL MYITHRDNPL SEEELAKSLE
FGTTLAAARA SLGDIRGPDD YKVGLKVPFN ERSEYVKLRF EEAKSRLRMR EYKVVVIPTR
LVQNPVLTVG LGDTISAGAF LTYLEFLKRH
