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K6PF_THELI
ID   K6PF_THELI              Reviewed;         459 AA.
AC   Q977Q3;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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 litoralis.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=2265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Jeong J., Ito S., Fushinobu S., Wakagi T.;
RT   "Molecular characterization of ADP-dependent phosphofructokinase from a
RT   hyperthermophile.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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; AB050016; BAB69952.1; -; Genomic_DNA.
DR   RefSeq; WP_020953560.1; NC_022084.1.
DR   AlphaFoldDB; Q977Q3; -.
DR   SMR; Q977Q3; -.
DR   GeneID; 16548417; -.
DR   OMA; NRIFEFR; -.
DR   BRENDA; 2.7.1.146; 6302.
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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..459
FT                   /note="ADP-specific phosphofructokinase"
FT                   /id="PRO_0000184769"
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   459 AA;  52852 MW;  40852F75DB94E987 CRC64;
     MMEFLKDFQK MGIYLAYNVN VDAIVYLNEK HIESLIKEFG AENIKKRIDE YPREINEPLD
     FVARLIHALK TGKPQAVPLV SYEADKWFNS RFKYDFERIG GQVGVIANLL ANLDFNKVIA
     YSPLLGRKQA EMFVNRDNLL YPVVENGKLV LKKPLEAYRE DDPVKINRIF EFRAGTKFKL
     GDETIEVPYS GRFIVACRFE DFARIETSPE LKPYLPEIGE MVDGAILSGY QGLRRYYSDG
     KDANYYLRKA KEDIKLLKKK KDIKIHVEFA SIQDRELRKK VIYNIFPLVD SVGMDEAEIA
     HILSVLGYRE LSDRIFTYNR IEDAVLGAKI LLDELNLEIL QVHTIYYLMY ITHNDNPLTE
     EELTKSLEVG TTLAAARAFL GDIKRPEDVK VGLNIPFNEK GEYVKLRFEE AKAKMRTREY
     KIVIIPTRLV RNPVSTVGLG DTISAGAFAS YLSLLKRKE
 
 
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