ID   PGK1_HORSE              Reviewed;         417 AA.
AC   P00559;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=Phosphoglycerate kinase 1;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P00558};
DE            EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558};
GN   Name=PGK1; Synonyms=PGK;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-417, AND SUBCELLULAR LOCATION.
RC   TISSUE=Muscle;
RX   PubMed=7287713; DOI=10.1016/s0021-9258(19)68618-7;
RA   Merrett M.;
RT   "Primary structure of 3-phosphoglycerate kinase from horse muscle. II.
RT   Amino acid sequence of cyanogen bromide peptides CB1-CB4 and CB6-CB14,
RT   sequence of methionine-containing regions, and complete sequence of the
RT   enzyme.";
RL   J. Biol. Chem. 256:10293-10305(1981).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC   TISSUE=Muscle;
RX   PubMed=450128; DOI=10.1038/279773a0;
RA   Banks R.D., Blake C.C.F., Evans P.R., Haser R., Rice D.W., Hardy G.W.,
RA   Merrett M., Phillips A.W.;
RT   "Sequence, structure and activity of phosphoglycerate kinase: a possible
RT   hinge-bending enzyme.";
RL   Nature 279:773-777(1979).
CC   -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the
CC       glycolytic pathway via the reversible conversion of 1,3-
CC       diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of
CC       purine and pyrimidine nucleotides can be used as substrates, but the
CC       activity is much lower on pyrimidines. In addition to its role as a
CC       glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha
CC       cofactor protein (primer recognition protein). Acts as a protein kinase
CC       when localized to the mitochondrion where it phosphorylates pyruvate
CC       dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex
CC       activity and suppress the formation of acetyl-coenzyme A from pyruvate,
CC       and consequently inhibit oxidative phosphorylation and promote
CC       glycolysis. May play a role in sperm motility.
CC       {ECO:0000250|UniProtKB:P00558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14802;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14803;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P00558};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBUNIT: Monomer. Interacts with kinase MAPK1/ERK2; the interaction is
CC       direct, occurs under hypoxic conditions, and promotes its interaction
CC       with PIN1. Interacts with peptidyl-prolyl cis-trans isomerase PIN1; the
CC       interaction is direct, occurs under hypoxic conditions, and targets the
CC       protein to the mitochondrion by promoting interactions with the TOM
CC       complex. Interacts with mitochondrial circRNA mcPGK1 (via its 2nd stem-
CC       loop); the interaction is direct and targets the protein to the
CC       mitochondrion by promoting interactions with the TOM complex. Interacts
CC       with pyruvate dehydrogenase kinase PDK1; the interaction is direct,
CC       occurs under hypoxic conditions and leads to PDK1-mediated inhibition
CC       of pyruvate dehydrogenase complex activity.
CC       {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P00558}. Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P00558}. Note=Hypoxic conditions promote
CC       mitochondrial targeting. Targeted to the mitochondrion following
CC       phosphorylation by MAPK1/ERK2, cis-trans isomerization by PIN1, and
CC       binding to mitochondrial circRNA mcPGK1.
CC       {ECO:0000250|UniProtKB:P00558}.
CC   -!- PTM: Phosphorylated at Ser-203 by MAPK1/ERK2 under hypoxic conditions,
CC       which promotes its mitochondrial targeting.
CC       {ECO:0000250|UniProtKB:P00558}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   PIR; A92292; KIHOG.
DR   PDB; 2PGK; X-ray; 3.00 A; A=-.
DR   AlphaFoldDB; P00559; -.
DR   SMR; P00559; -.
DR   FunCoup; P00559; 1001.
DR   STRING; 9796.ENSECAP00000012929; -.
DR   PaxDb; 9796-ENSECAP00000012929; -.
DR   PeptideAtlas; P00559; -.
DR   InParanoid; P00559; -.
DR   SABIO-RK; P00559; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   FunFam; 3.40.50.1260:FF:000019; Phosphoglycerate kinase 1; 1.
DR   FunFam; 3.40.50.1260:FF:000031; Phosphoglycerate kinase 1; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF14; PHOSPHOGLYCERATE KINASE 1; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR   PDBsum; 2PGK; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Hydroxylation; Kinase; Magnesium;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00558,
FT                   ECO:0000269|PubMed:7287713"
FT   CHAIN           2..417
FT                   /note="Phosphoglycerate kinase 1"
FT                   /id="PRO_0000145829"
FT   REGION          2..186
FT                   /note="Globular domain-1"
FT   REGION          38..43
FT                   /note="Mitochondrial targeting region exposed following
FT                   cis-trans isomerization by PIN1 and recognized by the TOM
FT                   complex for mitochondrial translocation of the protein"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   REGION          187..190
FT                   /note="Linker"
FT   REGION          191..417
FT                   /note="Globular domain-2"
FT   REGION          406..417
FT                   /note="Associated with globular domain 1"
FT   BINDING         23
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         24
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         25
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         26
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         38
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         39
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         62
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         63
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         65
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         66
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         122
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         123
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         170
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         171
FT                   /ligand="(2R)-3-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58272"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         214
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         214
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         215
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         216
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         219
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         220
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         238
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         238
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         239
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         313
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         338
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         340
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         343
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         343
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         344
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         6
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         48
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         97
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         131
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         191
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         196
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         199
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         216
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         220
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         267
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         291
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         323
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         361
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
SQ   SEQUENCE   417 AA;  44603 MW;  5110E246AF96931A CRC64;
     MSLSNKLTLD KLNVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
     MSHLGRPDVG PMPDKYSLQP VAVELKSLLG KDVLFLKDCV GPEVEKACAD PAAGSVILLE
     NLRFHVEEEG KGKDASGNKV KAEPAKIETF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
     LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
     AFTFLKVLNN MEIGTSLFDE EGAKIVKNLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
     ATVASGIPAG WMGLDCGTES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV
     KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV
//