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Database: UniProt/SWISS-PROT
Entry: PFKAM_RAT
LinkDB: PFKAM_RAT
Original site: PFKAM_RAT 
ID   PFKAM_RAT               Reviewed;         780 AA.
AC   P47858; Q63736;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 150.
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; Synonyms=Pfk-m;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Pancreatic islet;
RX   PubMed=8764833; DOI=10.1016/0167-4781(96)00088-7;
RA   Ma Z., Ramanadham S., Turk J., Kempe K., Hu Z., Ladenson J.;
RT   "Characterization of expression of phosphofructokinase isoforms in
RT   isolated rat pancreatic islets and purified beta cells and cloning and
RT   expression of the rat phosphofructokinase-A isoform.";
RL   Biochim. Biophys. Acta 1308:151-163(1996).
RN   [2]
RP   SEQUENCE REVISION TO 163-170 AND 494-498.
RA   Ma Z.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-213.
RC   STRAIN=Sprague-Dawley;
RA   Nakajima H.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-377 AND
RP   SER-775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- 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; U25651; AAC52786.1; -; mRNA.
DR   EMBL; D21869; BAA21013.1; -; mRNA.
DR   PIR; S71429; S71429.
DR   RefSeq; NP_113903.1; NM_031715.1.
DR   UniGene; Rn.11004; -.
DR   ProteinModelPortal; P47858; -.
DR   SMR; P47858; -.
DR   BioGrid; 249268; 3.
DR   ComplexPortal; CPX-2050; 6-phosphofructokinase, M4 homotetramer.
DR   ComplexPortal; CPX-2058; 6-phosphofructokinase, ML3 heterotetramer.
DR   ComplexPortal; CPX-2059; 6-phosphofructokinase, M2L2 heterotetramer.
DR   ComplexPortal; CPX-2060; 6-phosphofructokinase, M3L heterotetramer.
DR   IntAct; P47858; 2.
DR   MINT; P47858; -.
DR   STRING; 10116.ENSRNOP00000013374; -.
DR   iPTMnet; P47858; -.
DR   PhosphoSitePlus; P47858; -.
DR   jPOST; P47858; -.
DR   PaxDb; P47858; -.
DR   PRIDE; P47858; -.
DR   GeneID; 65152; -.
DR   KEGG; rno:65152; -.
DR   UCSC; RGD:68419; rat.
DR   CTD; 5213; -.
DR   RGD; 68419; Pfkm.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P47858; -.
DR   KO; K00850; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; P47858; -.
DR   SABIO-RK; P47858; -.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:P47858; -.
DR   Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR   GO; GO:0016208; F:AMP binding; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IDA:RGD.
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:0008443; F:phosphofructokinase activity; IMP:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0001678; P:cellular glucose homeostasis; NAS:RGD.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:RGD.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:RGD.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IBA:GO_Central.
DR   GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
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   1: Evidence at protein 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    780       ATP-dependent 6-phosphofructokinase,
FT                                muscle type.
FT                                /FTId=PRO_0000112020.
FT   NP_BIND      88     89       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     118    121       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        2    390       N-terminal catalytic PFK domain 1.
FT   REGION      164    166       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      208    210       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      298    301       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      391    401       Interdomain linker.
FT   REGION      402    780       C-terminal regulatory PFK domain 2.
FT   REGION      528    532       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      573    575       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      661    664       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       119    119       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      25     25       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     201    201       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     292    292       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     471    471       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     566    566       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     629    629       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     655    655       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     735    735       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     133    133       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     377    377       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     775    775       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    530    530       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   CONFLICT     33     33       T -> A (in Ref. 3; BAA21013).
FT                                {ECO:0000305}.
FT   CONFLICT     46     46       L -> A (in Ref. 3; BAA21013).
FT                                {ECO:0000305}.
FT   CONFLICT    150    150       R -> A (in Ref. 3; BAA21013).
FT                                {ECO:0000305}.
FT   CONFLICT    160    160       F -> G (in Ref. 3; BAA21013).
FT                                {ECO:0000305}.
FT   CONFLICT    180    180       S -> F (in Ref. 3; BAA21013).
FT                                {ECO:0000305}.
SQ   SEQUENCE   780 AA;  85560 MW;  CECC3995C4F271FA CRC64;
     MTHEEHHEAK TLGIGKAIAV LTSGGDAQGM NATVRAVVRV GIFTGLRVFF VHEGYQGLVD
     GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
     SLTGADTFRS EWSDLLNDLQ KDGKITAEER TKSSYLNIVF LVGSIDNDFC GTDMTIGTDS
     ALHRIVEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
     EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
     RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NTAVRLPLME CVQVTKDVTK
     AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL HTVAVMNVGA PAAGMNAAVR
     STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ
     ISANITKYNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI
     GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
     TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
     HMQQGGNPTP FDRNFATKMG AKATNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
     QPVTELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
//
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