ID   PFKA_CALFI              Reviewed;         184 AA.
AC   Q27543;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase;
DE            Short=ATP-PFK;
DE            Short=Phosphofructokinase;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphohexokinase;
DE   Flags: Fragment;
GN   Name=PFK;
OS   Calanus finmarchicus (Calanus tonsus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Hexanauplia; Copepoda; Calanoida; Calanidae; Calanus.
OX   NCBI_TaxID=6837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7670600;
RA   Crawford D.L.;
RT   "Nuclear genes from the copepod Calanus finmarchicus.";
RL   Mol. Mar. Biol. Biotechnol. 4:241-247(1995).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000250|UniProtKB:P16861}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000250|UniProtKB:P16861};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P16861};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {ECO:0000250|UniProtKB:P16861}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000250|UniProtKB:P16861}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P16861}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16861}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC       sub-subfamily. {ECO:0000305}.
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DR   EMBL; U21244; AAA85287.1; -; mRNA.
DR   AlphaFoldDB; Q27543; -.
DR   SMR; Q27543; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.460; -; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           <1..>184
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000112028"
FT   REGION          <1..>184
FT                   /note="N-terminal catalytic PFK domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         2..5
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         3
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         48..50
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         92..94
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   BINDING         182..>184
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P16861"
FT   NON_TER         1
FT   NON_TER         184
SQ   SEQUENCE   184 AA;  20208 MW;  E9B71F095A5DF2AD CRC64;
     GGDGSLTGAN RFKGEWSSLV KELLETGKIT KEVAEKHSHL NIVGMVGSID NDFCGTDMTI
     GTDSALHRIV EVADNIIPTA YSHQRAFVLE VMGRHCGYLA LVAGIVTEAD FVFAPEWPPE
     EDWPEKLCKK LELERQSGQR LNIIIVAEGA IDRQGNPITA EGVKKIIVDR LEMDTRTTVL
     GHIQ