ID PFKAM_PIG Reviewed; 780 AA.
AC Q2HYU2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 13-FEB-2019, entry version 70.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Deng C.Y., Xiong Y.Z.;
RT "Cloning and characterization of porcine phosphofructokinase, muscle
RT (PFKM).";
RL Submitted (JAN-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; DQ363336; ABC94908.1; -; mRNA.
DR RefSeq; NP_001038015.1; NM_001044550.1.
DR UniGene; Ssc.4741; -.
DR ProteinModelPortal; Q2HYU2; -.
DR SMR; Q2HYU2; -.
DR STRING; 9823.ENSSSCP00000021675; -.
DR PaxDb; Q2HYU2; -.
DR PeptideAtlas; Q2HYU2; -.
DR PRIDE; Q2HYU2; -.
DR GeneID; 733601; -.
DR KEGG; ssc:733601; -.
DR CTD; 5213; -.
DR eggNOG; KOG2440; Eukaryota.
DR eggNOG; COG0205; LUCA.
DR HOVERGEN; HBG000976; -.
DR InParanoid; Q2HYU2; -.
DR KO; K00850; -.
DR OrthoDB; 172878at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008227; 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; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
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:0046716; P:muscle cell cellular homeostasis; 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 2 780 ATP-dependent 6-phosphofructokinase,
FT muscle type.
FT /FTId=PRO_0000289804.
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 377 377 Phosphoserine.
FT {ECO:0000250|UniProtKB:P47857}.
FT MOD_RES 667 667 Phosphoserine.
FT {ECO:0000250|UniProtKB:P08237}.
FT MOD_RES 775 775 Phosphoserine.
FT {ECO:0000250|UniProtKB:P00511}.
FT CARBOHYD 530 530 O-linked (GlcNAc) serine. {ECO:0000250}.
SQ SEQUENCE 780 AA; 85327 MW; C9E127CBFF6005B9 CRC64;
MTHEEHHAAK SLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIYTGARVFF VHEGYQGLVD
GGDNIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
SLTGADTFRS EWGDLLNDLQ KAGKITAEEA NKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
ALHRIIEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDAWE
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GQLITSENIK DLVVKRLGYD TRVTVLGHVQ
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
AMNEKRFDEA MKLRGRSFMN NWEVYKLLAH VRPPVTKSGS YTVAVMNVGA PTAGMNAAVR
STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQYDELCI PFVVIPATVS NNVPGSDFSV
GADTALNTIC MTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
HMQQGGSPTP LDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
QPVTELKEQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSEHAHLEHI TRKRSGEATI
//
