PGK1_PIG
ID PGK1_PIG Reviewed; 417 AA.
AC Q7SIB7; Q6B6L7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
GN Name=PGK1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Xu D.Q., Xiong Y.Z.;
RT "Molecular cloning and characterization of porcine PGK1.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-417 IN COMPLEX WITH SUBSTRATE
RP AND AMP.
RX PubMed=11178909; DOI=10.1006/jmbi.2000.4294;
RA Szilagyi A.N., Ghosh M., Garman E., Vas M.;
RT "A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with
RT bound MgADP and 3-phosphoglycerate in open conformation: new insight into
RT the role of the nucleotide in domain closure.";
RL J. Mol. Biol. 306:499-511(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=12102622; DOI=10.1021/bi020210j;
RA Kovari Z., Flachner B., Naray-Szabo G., Vas M.;
RT "Crystallographic and thiol-reactivity studies on the complex of pig muscle
RT phosphoglycerate kinase with ATP analogues: correlation between nucleotide
RT binding mode and helix flexibility.";
RL Biochemistry 41:8796-8806(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
RX PubMed=15035615; DOI=10.1021/bi035022n;
RA Flachner B., Kovari Z., Varga A., Gugolya Z., Vonderviszt F.,
RA Naray-Szabo G., Vas M.;
RT "Role of phosphate chain mobility of MgATP in completing the 3-
RT phosphoglycerate kinase catalytic site: binding, kinetic, and
RT crystallographic studies with ATP and MgATP.";
RL Biochemistry 43:3436-3449(2004).
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:0000269|PubMed:11178909,
CC ECO:0000269|PubMed:15035615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=The sequence shown in PDB entry 1KF0 is a tentative sequence based on the electron density. It differs from that shown in 14 positions.; Evidence={ECO:0000305};
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DR EMBL; AY677198; AAT77773.1; -; mRNA.
DR RefSeq; NP_001093402.1; NM_001099932.1.
DR PDB; 1HDI; X-ray; 1.80 A; A=5-417.
DR PDB; 1KF0; X-ray; 2.50 A; A=2-417.
DR PDB; 1VJC; X-ray; 2.10 A; A=2-417.
DR PDB; 1VJD; X-ray; 1.90 A; A=2-417.
DR PDBsum; 1HDI; -.
DR PDBsum; 1KF0; -.
DR PDBsum; 1VJC; -.
DR PDBsum; 1VJD; -.
DR AlphaFoldDB; Q7SIB7; -.
DR SMR; Q7SIB7; -.
DR STRING; 9823.ENSSSCP00000013238; -.
DR PaxDb; Q7SIB7; -.
DR PeptideAtlas; Q7SIB7; -.
DR PRIDE; Q7SIB7; -.
DR GeneID; 407608; -.
DR KEGG; ssc:407608; -.
DR CTD; 5230; -.
DR eggNOG; KOG1367; Eukaryota.
DR InParanoid; Q7SIB7; -.
DR OrthoDB; 838642at2759; -.
DR BRENDA; 2.7.2.3; 6170.
DR SABIO-RK; Q7SIB7; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; Q7SIB7; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS: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; Glycolysis;
KW Hydroxylation; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CHAIN 2..417
FT /note="Phosphoglycerate kinase 1"
FT /id="PRO_0000145837"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11178909"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11178909"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11178909"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11178909"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11178909"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15035615"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15035615"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15035615"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15035615"
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"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1VJD"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1HDI"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1VJC"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1HDI"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1HDI"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:1HDI"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1HDI"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:1HDI"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:1HDI"
SQ SEQUENCE 417 AA; 44559 MW; B014E769058C1135 CRC64;
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAIPSIKFC LDNGAKSVVL
MSHLGRPDGI PMPDKYSLEP VAVELKSLPG KDVLFLKDCV GPEVEKACAD PAAGSVILLE
NLRFHVEEEG KGKDASGSKV KADPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPKKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
AFTFLKVLNN MEIGTSLFDE EGSKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKIGQ
ATVASGIPAG WMGLDCGPES SKKYSEAVAR AKQIVWNGPV GVFEWEAFAQ GTKALMDEVV
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV
