K6PF_METJA
ID K6PF_METJA Reviewed; 462 AA.
AC Q58999;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bifunctional ADP-specific glucokinase/phosphofructokinase;
DE EC=2.7.1.146;
DE EC=2.7.1.147;
DE AltName: Full=ADP-GK;
DE AltName: Full=ADP-GK/PFK;
DE AltName: Full=ADP-Pfk;
DE AltName: Full=ADP-dependent glucokinase;
DE AltName: Full=ADP-dependent phosphofructokinase;
GN Name=pfkC; Synonyms=glkA; OrderedLocusNames=MJ1604;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11717273; DOI=10.1128/jb.183.24.7145-7153.2001;
RA Verhees C.H., Tuininga J.E., Kengen S.W.M., Stams A.J.M., van der Oost J.,
RA de Vos W.M.;
RT "ADP-dependent phosphofructokinases in mesophilic and thermophilic
RT methanogenic archaea.";
RL J. Bacteriol. 183:7145-7153(2001).
RN [3]
RP CHARACTERIZATION, AND ENZYME KINETICS.
RX PubMed=11856730; DOI=10.1074/jbc.c200059200;
RA Sakuraba H., Yoshioka I., Koga S., Takahashi M., Kitahama Y., Satomura T.,
RA Kawakami R., Ohshima T.;
RT "ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional enzyme
RT from the hyperthermophilic archaeon Methanococcus jannaschii.";
RL J. Biol. Chem. 277:12495-12498(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate and D-
CC glucose to fructose 1,6-bisphosphate and D-glucose 6-phosphate,
CC respectively, using ADP as the phosphate donor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.1.147;
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for D-glucose;
CC KM=0.032 mM for ADP with D-glucose as phosphoryl group acceptor;
CC KM=9.6 uM for fructose 6-phosphate;
CC KM=0.49 mM for ADP with D-fructose 6-phosphate as phosphoryl group
CC acceptor;
CC Vmax=11.2 umol/min/mg enzyme toward fructose 6-phosphate;
CC Vmax=9.59 umol/min/mg enzyme toward ADP;
CC pH dependence:
CC Optimum pH is 6.5.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99627.1; -; Genomic_DNA.
DR PIR; C64500; C64500.
DR PDB; 5OD2; X-ray; 1.98 A; A/B/C=4-461.
DR PDBsum; 5OD2; -.
DR AlphaFoldDB; Q58999; -.
DR SMR; Q58999; -.
DR STRING; 243232.MJ_1604; -.
DR EnsemblBacteria; AAB99627; AAB99627; MJ_1604.
DR KEGG; mja:MJ_1604; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR InParanoid; Q58999; -.
DR OMA; NRIFEFR; -.
DR PhylomeDB; Q58999; -.
DR BRENDA; 2.7.1.146; 3260.
DR BRENDA; 2.7.1.147; 3260.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..462
FT /note="Bifunctional ADP-specific
FT glucokinase/phosphofructokinase"
FT /id="PRO_0000184764"
FT DOMAIN 1..458
FT /note="ADPK"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 365..385
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:5OD2"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:5OD2"
FT HELIX 440..460
FT /evidence="ECO:0007829|PDB:5OD2"
SQ SEQUENCE 462 AA; 53362 MW; D91088B60DBAB104 CRC64;
MCDIMEIKKF IETIKGTKLF TAYNTNVDAI KYLKDEDVQK LVDEFNHKDI IERMEEYPRI
IEEPLDFVAR LVHSIKTGKP AEVPIKDDKK LHEWFDRIKY DEERMGGQAG IVSNLMATLQ
IDKIIVYTPF LSKKQAEMFV DYDNLLYPLV ENGNLVLKKV REAYRDDPIK INRIFEFKKG
LKFKLNGEEI TAKQSTRFIV ASRPEALRIE IKDDVRKFLP KIGEAVDCAF LSGYQAIKEE
YRDGKTAKYY FERAEEDIKL LKKNKNIKTH LEFASISNIE IRKMVVDYIL SNVESVGMDE
TEIANVLHIL GYDELSNNIL KDSFIEDVIE GAKILLDKFK NLEVVQVHTI YYILFVCRAD
NPLSKEELEE CLEFSTILAS TKAKLGNIRA IDDLHEGLKI PHNKYGDLLK EIAEKFNDNN
YKIALSPSRY VEKPKSTVGL GDTISSGAFV YYVSLLNKKR MS
