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Pyruvate kinase PKM (EC 2.7.1.40) (Pyruvate kinase muscle isozyme)

 KPYM_RABIT              Reviewed;         531 AA.
P11974; O18919; Q29501;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
10-OCT-2018, entry version 166.
RecName: Full=Pyruvate kinase PKM;
EC=2.7.1.40;
AltName: Full=Pyruvate kinase muscle isozyme;
Name=PKM; Synonyms=PKM2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M1), AND X-RAY CRYSTALLOGRAPHY
(2.9 ANGSTROMS) IN COMPLEX WITH MANGANESE AND PAOTASSIUM IONS AND
PYRUVATE.
TISSUE=Skeletal muscle;
PubMed=8193145; DOI=10.1021/bi00186a033;
Larsen T.M., Laughlin L.T., Holden H.M., Rayment I., Reed G.H.;
"Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+,
and pyruvate.";
Biochemistry 33:6301-6309(1994).
[2]
SEQUENCE REVISION TO 234-235.
Laughlin L.T.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M1).
PubMed=8626426; DOI=10.1074/jbc.271.11.6313;
Cheng X., Friesen R.H.E., Lee J.C.;
"Effects of conserved residues on the regulation of rabbit muscle
pyruvate kinase.";
J. Biol. Chem. 271:6313-6321(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
TISSUE=Kidney;
PubMed=9485447; DOI=10.1021/bi971990c;
Friesen R.H.E., Chin A.J., Ledman D.W., Lee J.C.;
"Interfacial communications in recombinant rabbit kidney pyruvate
kinase.";
Biochemistry 37:2949-2960(1998).
[5]
PROTEIN SEQUENCE OF 343-376.
PubMed=3813559; DOI=10.1016/0003-9861(87)90645-X;
Bezares G., Eyzaguirre J., Hinrichs M.V., Heinrikson R.L., Reardon I.,
Kemp R.G., Latshaw S.P., Bazaes S.;
"Isolation and sequence determination of an active site peptide of
rabbit muscle pyruvate kinase.";
Arch. Biochem. Biophys. 253:133-137(1987).
[6]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH
L-PHOSPHOLACTATE, AND MAGNESIUM AND POTASSIUM IONS.
TISSUE=Skeletal muscle;
PubMed=9308890; DOI=10.1006/abbi.1997.0257;
Larsen T.M., Benning M.M., Wesenberg G.E., Rayment I., Reed G.H.;
"Ligand-induced domain movement in pyruvate kinase: structure of the
enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7-A
resolution.";
Arch. Biochem. Biophys. 345:199-206(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH OXYLATE AND
MAGNESIUM IONS.
TISSUE=Skeletal muscle;
PubMed=9572839; DOI=10.1021/bi980243s;
Larsen T.M., Benning M.M., Rayment I., Reed G.H.;
"Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle
pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.";
Biochemistry 37:6247-6255(1998).
-!- FUNCTION: Glycolytic enzyme that catalyzes the transfer of a
phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating
ATP. Stimulates POU5F1-mediated transcriptional activation (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
-!- ACTIVITY REGULATION: Isoform M2 is allosterically activated by D-
fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-
triiodo-L-thyronine (T3). The activity of the tetrameric form is
inhibited by PML. Selective binding to tyrosine-phosphorylated
peptides releases the allosteric activator FBP, leading to
inhibition of PKM enzymatic activity, this diverts glucose
metabolites from energy production to anabolic processes when
cells are stimulated by certain growth factors. Glycolytic flux
are highly dependent on de novo biosynthesis of serine and
glycine, and serine is a natural ligand and allosteric activator
of isoform M2 (By similarity). {ECO:0000250}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 5/5.
-!- SUBUNIT: Monomer and homotetramer. Exists as a monomer in the
absence of fructose 1,6 bi-phosphate (FBP), and reversibly
associates to form a homotetramer in the presence of FBP. The
monomeric form binds T3. Tetramer formation induces pyruvate
kinase activity. FBP stimulates the formation of tetramers from
dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform
M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and
enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the
interaction is enhanced by binding of EGLN3, promoting enhanced
transcription activity under hypoxia (By similarity). Interacts
(isoform M2, but not isoform M1) with TRIM35; this interaction
prevents FGFR1-dependent tyrosine phosphorylation (By similarity).
Interacts with JMJD8 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P14618}.
-!- INTERACTION:
P00563:CKM; NbExp=2; IntAct=EBI-7133357, EBI-2750756;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14618}.
Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the
nucleus in response to different apoptotic stimuli. Nuclear
translocation is sufficient to induce cell death that is caspase
independent, isoform-specific and independent of its enzymatic
activity. {ECO:0000250|UniProtKB:P14618}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=M1; Synonyms=PKM1;
IsoId=P11974-1; Sequence=Displayed;
Name=M2; Synonyms=PKM2;
IsoId=P11974-2, O18919-1;
Sequence=VSP_011106;
-!- PTM: ISGylated. {ECO:0000250}.
-!- PTM: Acetylation at Lys-305 is stimulated by high glucose
concentration, it decreases enzyme activity and promotes its
lysosomal-dependent degradation via chaperone-mediated autophagy.
{ECO:0000250}.
-!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals
(L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L
and R isozymes are generated from the PKLR by differential
splicing of RNA; the M1 and M2 forms are produced from the PKM
gene by differential splicing. L type is major isozyme in the
liver, R is found in red cells, M1 is the main form in muscle,
heart and brain, and M2 is found in early fetal tissues as well as
in most cancer cells.
-!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/PKL/";
-----------------------------------------------------------------------
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EMBL; U09028; AAB61963.1; -; mRNA.
EMBL; U44751; AAC48536.1; -; mRNA.
EMBL; AF032389; AAB86587.1; -; mRNA.
PIR; A28506; A28506.
PIR; A54113; A54113.
RefSeq; NP_001182573.1; NM_001195644.1.
RefSeq; NP_001182574.1; NM_001195645.1. [P11974-2]
UniGene; Ocu.2156; -.
PDB; 1A49; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-531.
PDB; 1A5U; X-ray; 2.35 A; A/B/C/D/E/F/G/H=2-531.
PDB; 1AQF; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-531.
PDB; 1F3W; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-531.
PDB; 1F3X; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-531.
PDB; 1PKN; X-ray; 2.90 A; A=2-531.
PDB; 2G50; X-ray; 1.65 A; A/B/C/D/E/F/G/H=2-531.
PDB; 3N25; X-ray; 2.41 A; A/B/C/D/E/F/G/H=1-531.
PDBsum; 1A49; -.
PDBsum; 1A5U; -.
PDBsum; 1AQF; -.
PDBsum; 1F3W; -.
PDBsum; 1F3X; -.
PDBsum; 1PKN; -.
PDBsum; 2G50; -.
PDBsum; 3N25; -.
ProteinModelPortal; P11974; -.
SMR; P11974; -.
DIP; DIP-47514N; -.
IntAct; P11974; 1.
MINT; P11974; -.
ChEMBL; CHEMBL5637; -.
PRIDE; P11974; -.
GeneID; 100008676; -.
KEGG; ocu:100008676; -.
CTD; 5315; -.
HOGENOM; HOG000021559; -.
HOVERGEN; HBG000941; -.
InParanoid; P11974; -.
KO; K00873; -.
BRENDA; 2.7.1.40; 1749.
SABIO-RK; P11974; -.
UniPathway; UPA00109; UER00188.
EvolutionaryTrace; P11974; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
CDD; cd00288; Pyruvate_Kinase; 1.
Gene3D; 2.40.33.10; -; 1.
Gene3D; 3.40.1380.20; -; 2.
InterPro; IPR001697; Pyr_Knase.
InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
InterPro; IPR018209; Pyrv_Knase_AS.
InterPro; IPR015793; Pyrv_Knase_brl.
InterPro; IPR015795; Pyrv_Knase_C.
InterPro; IPR036918; Pyrv_Knase_C_sf.
InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
PANTHER; PTHR11817; PTHR11817; 1.
Pfam; PF00224; PK; 1.
Pfam; PF02887; PK_C; 1.
PRINTS; PR01050; PYRUVTKNASE.
SUPFAM; SSF50800; SSF50800; 1.
SUPFAM; SSF51621; SSF51621; 2.
SUPFAM; SSF52935; SSF52935; 1.
TIGRFAMs; TIGR01064; pyruv_kin; 1.
PROSITE; PS00110; PYRUVATE_KINASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Glycolysis; Isopeptide bond; Kinase; Magnesium; Metal-binding;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Potassium;
Pyruvate; Reference proteome; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11979}.
CHAIN 2 531 Pyruvate kinase PKM.
/FTId=PRO_0000112091.
REGION 307 531 Interaction with POU5F1. {ECO:0000250}.
REGION 432 437 D-fructose 1,6-bisphosphate binding; part
of allosteric site. {ECO:0000250}.
REGION 514 521 D-fructose 1,6-bisphosphate binding; part
of allosteric site. {ECO:0000250}.
METAL 75 75 Potassium. {ECO:0000250}.
METAL 77 77 Potassium. {ECO:0000250}.
METAL 113 113 Potassium. {ECO:0000250}.
METAL 114 114 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 272 272 Magnesium. {ECO:0000250}.
METAL 296 296 Magnesium. {ECO:0000250}.
BINDING 70 70 Serine. {ECO:0000250}.
BINDING 73 73 Substrate. {ECO:0000250}.
BINDING 106 106 Serine. {ECO:0000250}.
BINDING 295 295 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 296 296 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 328 328 Substrate. {ECO:0000250}.
BINDING 464 464 Serine. {ECO:0000250}.
BINDING 482 482 D-fructose 1,6-bisphosphate; part of
allosteric site. {ECO:0000250}.
BINDING 489 489 D-fructose 1,6-bisphosphate; part of
allosteric site. {ECO:0000250}.
SITE 270 270 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P11979}.
MOD_RES 3 3 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 41 41 Phosphothreonine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 66 66 N6-succinyllysine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 89 89 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P11980}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P11980}.
MOD_RES 105 105 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 148 148 Phosphotyrosine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 166 166 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 166 166 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 175 175 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 195 195 Phosphothreonine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 266 266 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 270 270 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14618}.
MOD_RES 322 322 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 322 322 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 475 475 N6-acetyllysine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 498 498 N6-succinyllysine.
{ECO:0000250|UniProtKB:P52480}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P14618}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P14618}.
CROSSLNK 266 266 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P14618}.
CROSSLNK 270 270 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P14618}.
VAR_SEQ 389 433 MFHRKLFEELARSSSHSTDLMEAMAMGSVEASYKCLAAALI
VLTE -> IYHLQLFEELRRLAPITSDPTEAAAVGAVEASF
KCCSGAIIVLTK (in isoform M2).
{ECO:0000303|PubMed:9485447}.
/FTId=VSP_011106.
CONFLICT 401 401 S -> A (in Ref. 3; AAC48536).
{ECO:0000305}.
HELIX 18 21 {ECO:0000244|PDB:2G50}.
HELIX 26 31 {ECO:0000244|PDB:2G50}.
STRAND 45 50 {ECO:0000244|PDB:2G50}.
TURN 53 55 {ECO:0000244|PDB:2G50}.
HELIX 58 67 {ECO:0000244|PDB:2G50}.
STRAND 71 75 {ECO:0000244|PDB:2G50}.
HELIX 81 96 {ECO:0000244|PDB:2G50}.
TURN 97 100 {ECO:0000244|PDB:2G50}.
TURN 102 104 {ECO:0000244|PDB:2G50}.
STRAND 109 113 {ECO:0000244|PDB:2G50}.
STRAND 119 121 {ECO:0000244|PDB:2G50}.
STRAND 126 128 {ECO:0000244|PDB:2G50}.
STRAND 130 134 {ECO:0000244|PDB:2G50}.
STRAND 139 143 {ECO:0000244|PDB:2G50}.
HELIX 146 148 {ECO:0000244|PDB:2G50}.
STRAND 154 160 {ECO:0000244|PDB:2G50}.
HELIX 164 167 {ECO:0000244|PDB:2G50}.
STRAND 173 176 {ECO:0000244|PDB:2G50}.
TURN 177 180 {ECO:0000244|PDB:2G50}.
STRAND 181 189 {ECO:0000244|PDB:2G50}.
STRAND 192 199 {ECO:0000244|PDB:2G50}.
STRAND 201 203 {ECO:0000244|PDB:2G50}.
STRAND 208 210 {ECO:0000244|PDB:2G50}.
STRAND 212 214 {ECO:0000244|PDB:3N25}.
HELIX 223 234 {ECO:0000244|PDB:2G50}.
STRAND 238 242 {ECO:0000244|PDB:2G50}.
HELIX 248 258 {ECO:0000244|PDB:2G50}.
TURN 259 264 {ECO:0000244|PDB:2G50}.
STRAND 265 271 {ECO:0000244|PDB:2G50}.
HELIX 274 278 {ECO:0000244|PDB:2G50}.
HELIX 280 286 {ECO:0000244|PDB:2G50}.
STRAND 287 293 {ECO:0000244|PDB:2G50}.
HELIX 294 300 {ECO:0000244|PDB:2G50}.
HELIX 303 305 {ECO:0000244|PDB:2G50}.
HELIX 306 320 {ECO:0000244|PDB:2G50}.
STRAND 324 329 {ECO:0000244|PDB:2G50}.
HELIX 332 335 {ECO:0000244|PDB:2G50}.
STRAND 337 339 {ECO:0000244|PDB:1PKN}.
HELIX 342 354 {ECO:0000244|PDB:2G50}.
STRAND 357 362 {ECO:0000244|PDB:2G50}.
HELIX 363 366 {ECO:0000244|PDB:2G50}.
HELIX 371 387 {ECO:0000244|PDB:2G50}.
HELIX 391 401 {ECO:0000244|PDB:2G50}.
TURN 402 404 {ECO:0000244|PDB:2G50}.
HELIX 408 423 {ECO:0000244|PDB:2G50}.
STRAND 428 431 {ECO:0000244|PDB:2G50}.
STRAND 433 435 {ECO:0000244|PDB:2G50}.
HELIX 436 443 {ECO:0000244|PDB:2G50}.
STRAND 450 455 {ECO:0000244|PDB:2G50}.
HELIX 457 462 {ECO:0000244|PDB:2G50}.
HELIX 463 465 {ECO:0000244|PDB:2G50}.
STRAND 469 473 {ECO:0000244|PDB:2G50}.
HELIX 482 499 {ECO:0000244|PDB:2G50}.
STRAND 508 513 {ECO:0000244|PDB:2G50}.
STRAND 515 518 {ECO:0000244|PDB:1A49}.
STRAND 524 529 {ECO:0000244|PDB:2G50}.
SEQUENCE 531 AA; 58048 MW; AC0AFB579FC505E6 CRC64;
MSKSHSEAGS AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVET
LKEMIKSGMN VARMNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVDV GSKVYVDDGL
ISLQVKQKGP DFLVTEVENG GFLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV
FASFIRKAAD VHEVRKILGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
IPAEKVFLAQ KMIIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM
LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELAR SSSHSTDLME AMAMGSVEAS
YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNHQTA RQAHLYRGIF PVVCKDPVQE
AWAEDVDLRV NLAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P


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