ID   PFKAM_BOVIN             Reviewed;         779 AA.
AC   Q0IIG5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=PFK-M;
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=6-phosphofructokinase type A;
DE   AltName: Full=Phosphofructo-1-kinase isozyme A;
DE            Short=PFK-A;
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=PFKM;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_03184}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC       (PFK) enzyme functions as a tetramer composed of different combinations
CC       of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC       composition of the PFK tetramer differs according to the tissue type it
CC       is present in. The kinetic and regulatory properties of the tetrameric
CC       enzyme are dependent on the subunit composition, hence can vary across
CC       tissues (Probable). Interacts (via C-terminus) with HK1 (via N-terminal
CC       spermatogenic cell-specific region) (By similarity).
CC       {ECO:0000250|UniProtKB:P47857, ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
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:0000255|HAMAP-Rule:MF_03184}.
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DR   EMBL; BC122655; AAI22656.1; -; mRNA.
DR   RefSeq; NP_001068736.1; NM_001075268.1.
DR   AlphaFoldDB; Q0IIG5; -.
DR   SMR; Q0IIG5; -.
DR   CORUM; Q0IIG5; -.
DR   STRING; 9913.ENSBTAP00000066012; -.
DR   GlyCosmos; Q0IIG5; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000000359; -.
DR   PeptideAtlas; Q0IIG5; -.
DR   Ensembl; ENSBTAT00000000359.5; ENSBTAP00000000359.4; ENSBTAG00000000286.6.
DR   GeneID; 506544; -.
DR   KEGG; bta:506544; -.
DR   CTD; 5213; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000286; -.
DR   VGNC; VGNC:32774; PFKM.
DR   eggNOG; KOG2440; Eukaryota.
DR   GeneTree; ENSGT00940000155440; -.
DR   HOGENOM; CLU_011053_0_0_1; -.
DR   InParanoid; Q0IIG5; -.
DR   OMA; WHNLGGS; -.
DR   OrthoDB; 374214at2759; -.
DR   TreeFam; TF300411; -.
DR   Reactome; R-BTA-70171; Glycolysis.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000000286; Expressed in biceps femoris and 104 other cell types or tissues.
DR   ExpressionAtlas; Q0IIG5; baseline and differential.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   CDD; cd00764; Eukaryotic_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR041914; PFK_vert-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF59; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis;
KW   Glycoprotein; Hydroxylation; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00511"
FT   CHAIN           2..779
FT                   /note="ATP-dependent 6-phosphofructokinase, muscle type"
FT                   /id="PRO_0000284438"
FT   REGION          2..389
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          390..400
FT                   /note="Interdomain linker"
FT   REGION          401..779
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         87..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         117..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         163..165
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         207..209
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         297..300
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         470
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         527..531
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         565
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         572..574
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         628
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         654
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         660..663
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         734
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P00511"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47858"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47857"
FT   MOD_RES         556
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08237"
FT   MOD_RES         666
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08237"
FT   MOD_RES         774
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00511"
FT   CARBOHYD        529
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   779 AA;  85294 MW;  BBA2D207ADD079EE CRC64;
     MTHEHHAAKT LGIGKAIAVL TSGGDAQGMN AAVRAVVRVG IYTGARVFFV HEGYQGLVDG
     GDNIREATWE SVSMMLQLGG TVIGSARCKD FREREGRLRA AHNLVKRGIT NLCVIGGDGS
     LTGADTFRSE WSDLLSDLQK SGKITAEEAT KSSYLNIVGL VGSIDNDFCG TDMTIGTDSA
     LHRIIEIVDA ITTTAQSHQR TFVLEVMGRH CGYLALVTSL SCGADWVFIP ECPPDDDWEE
     HLCRRLSETR NRGSRLNIII VAEGAIDKNG KPITSEDIKN LVVKRLGYDT RVTVLGHVQR
     GGTPSAFDRI LGSRMGVEAV MALLEGTPDT PACVVSLSGN QAVRLPLMEC VQVTKDVTRA
     MDERRFDEAL KLRGRSFMNN WEVYKLLAHV RPPKSKSGSH TVAVMNVGAP AAGMNAAVRS
     TVRIGLIQGN RMLVVHDGFE GLAKGQIEEA GWSYVGGWTG QGGSKLGTKR TLPKKSFEQI
     SANITKFNIQ GLVIIGGFEA YTGGLELMEG RKQYDELCIP FVVIPATVSN NVPGSDFSVG
     ADTALNTICM TCDRIKQSAA GTKRRVFIIE TMGGYCGYLA TMAGLAAGAD AAYIFEDPFT
     IRDLQVNVEH LVQKMKTTVK RGLVLRNEKC NENYTTDFIF NLYSEEGKGI FDSRKNVLGH
     MQQGGSPTPF DRNFATKMGA KAMNWMSGKI KESYRNGRIF ANSPDSGCVL GMRKRALVFQ
     PVTELKEQTD FEHRIPKEQW WLKLRPILKI LAKYEIDLDT SEHAHLEHIS RKRSGEANV
//