PGK1_HORSE
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 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
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. 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). May play a role in sperm
CC motility. {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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7287713}.
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 PDBsum; 2PGK; -.
DR AlphaFoldDB; P00559; -.
DR SMR; P00559; -.
DR STRING; 9796.ENSECAP00000012929; -.
DR PaxDb; P00559; -.
DR PeptideAtlas; P00559; -.
DR PRIDE; P00559; -.
DR InParanoid; P00559; -.
DR SABIO-RK; P00559; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P00559; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Hydroxylation; Kinase;
KW Nucleotide-binding; Phosphoprotein; 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 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 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT BINDING 171
FT /ligand="substrate"
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 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 373..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
