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Database: UniProt
Entry: P52784
LinkDB: P52784
Original site: P52784 
ID   PFKAM_CANLF             Reviewed;         782 AA.
AC   P52784;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-SEP-2018, 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; Synonyms=M-PFK;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8654960; DOI=10.1016/0378-1119(95)00761-X;
RA   Smith B.F., Henthorn P.S., Rajpurohit Y., Stedman H., Wolfe J.H.,
RA   Patterson D.F., Giger U.;
RT   "A cDNA encoding canine muscle-type phosphofructokinase.";
RL   Gene 168:275-276(1996).
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: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {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; U25183; AAC48615.1; -; mRNA.
DR   RefSeq; NP_001003199.1; NM_001003199.1.
DR   UniGene; Cfa.3710; -.
DR   ProteinModelPortal; P52784; -.
DR   SMR; P52784; -.
DR   STRING; 9615.ENSCAFP00000013277; -.
DR   PaxDb; P52784; -.
DR   PRIDE; P52784; -.
DR   Ensembl; ENSCAFT00000046392; ENSCAFP00000037674; ENSCAFG00000009035.
DR   GeneID; 403849; -.
DR   KEGG; cfa:403849; -.
DR   CTD; 5213; -.
DR   VGNC; VGNC:44447; PFKM.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00390000013209; -.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P52784; -.
DR   KO; K00850; -.
DR   Reactome; R-CFA-70171; Glycolysis.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002254; Chromosome 27.
DR   Bgee; ENSCAFG00000009035; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
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   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    782       ATP-dependent 6-phosphofructokinase,
FT                                muscle type.
FT                                /FTId=PRO_0000112014.
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    403       Interdomain linker.
FT   REGION      404    782       C-terminal regulatory PFK domain 2.
FT   REGION      530    534       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      575    577       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      663    666       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     473    473       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     568    568       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     631    631       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     657    657       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     737    737       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:0000250|UniProtKB:P47858}.
FT   MOD_RES     377    377       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47857}.
FT   MOD_RES     669    669       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08237}.
FT   MOD_RES     777    777       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00511}.
FT   CARBOHYD    532    532       O-linked (GlcNAc) serine. {ECO:0000250}.
SQ   SEQUENCE   782 AA;  85561 MW;  7C28514057CFE1C9 CRC64;
     MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
     GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
     SLTGADTFRS EWSDLLSDLQ KAGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
     ALHRIIEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
     EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEEIK ELVVKRLGYD TRVTVLGHVQ
     RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
     AMNDRKFDEA MKLRGRSFMN NWEVYKLLAH IRPPVSKTSA TMHTVAVMNV GAPAAGMNAA
     VRSTVRIGLI QGNRVLVVHD GFEGLAKGQI EEAGWSYVGG WTGQGGSKLG TKRTLPKKSF
     EQISANITKF NIQGLIIIGG FEAYTGGLEL MEGRKQFDEL CIPFVVIPAT VSNNVPGSDF
     SVGADTALNT ICTTCDRIKQ SAAGTKRRVF IIETMGGYCG YLATMAGLAA GADAAYIFEE
     PFTIRDLQAN VEHLVQKMKT TVKRGLVLRN EKCNENYTTD FIFNLYSEEG KGIFDSRKNV
     LGHMQQGGSP TPFDRNFATK MGAKAMNWMS GKIKESYRNG RIFANTPDSG CVLGMRKRAL
     VFQPVTELKD QTDFDHRIPK EQWWLKLRPI LKILAKYEID LDTTEHAHLE HISRKRSGET
     SI
//
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