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Database: UniProt/SWISS-PROT
Entry: PFKAM_BOVIN
LinkDB: PFKAM_BOVIN
Original site: PFKAM_BOVIN 
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   05-DEC-2018, entry version 98.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       to 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
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic
CC       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)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
DR   EMBL; BC122655; AAI22656.1; -; mRNA.
DR   RefSeq; NP_001068736.1; NM_001075268.1.
DR   UniGene; Bt.61411; -.
DR   ProteinModelPortal; Q0IIG5; -.
DR   SMR; Q0IIG5; -.
DR   CORUM; Q0IIG5; -.
DR   STRING; 9913.ENSBTAP00000000359; -.
DR   PaxDb; Q0IIG5; -.
DR   PeptideAtlas; Q0IIG5; -.
DR   PRIDE; Q0IIG5; -.
DR   Ensembl; ENSBTAT00000000359; ENSBTAP00000000359; ENSBTAG00000000286.
DR   GeneID; 506544; -.
DR   KEGG; bta:506544; -.
DR   CTD; 5213; -.
DR   VGNC; VGNC:32774; PFKM.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000155440; -.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; Q0IIG5; -.
DR   KO; K00850; -.
DR   OMA; KQYDELC; -.
DR   OrthoDB; EOG091G01YN; -.
DR   TreeFam; TF300411; -.
DR   Reactome; R-BTA-70171; Glycolysis.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000000286; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097228; C:sperm principal piece; 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:0070061; F:fructose binding; IEA:Ensembl.
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:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; 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   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0093001; P:glycolysis from storage polysaccharide through glucose-1-phosphate; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IBA:GO_Central.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Cytoplasm; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00511}.
FT   CHAIN         2    779       ATP-dependent 6-phosphofructokinase,
FT                                muscle type.
FT                                /FTId=PRO_0000284438.
FT   NP_BIND      87     88       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     117    120       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        2    389       N-terminal catalytic PFK domain 1.
FT   REGION      163    165       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      207    209       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      297    300       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      390    400       Interdomain linker.
FT   REGION      401    779       C-terminal regulatory PFK domain 2.
FT   REGION      527    531       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      572    574       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      660    663       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    165    165       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       118    118       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      24     24       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     200    200       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     263    263       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     291    291       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     470    470       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     565    565       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     628    628       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     654    654       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     734    734       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       2      2       N-acetylthreonine.
FT                                {ECO:0000250|UniProtKB:P00511}.
FT   MOD_RES     132    132       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47858}.
FT   MOD_RES     376    376       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47857}.
FT   MOD_RES     666    666       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08237}.
FT   MOD_RES     774    774       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00511}.
FT   CARBOHYD    529    529       O-linked (GlcNAc) serine. {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
//
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