PGK1_CRIGR
ID PGK1_CRIGR Reviewed; 417 AA.
AC P50310;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoglycerate kinase 1;
DE EC=2.7.2.3;
GN Name=PGK1; Synonyms=PGK;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7604358; DOI=10.1007/bf02255824;
RA Hassan A.F., Morgan M.J., Faik P.;
RT "Characterization of cDNAs coding for glucose phosphate isomerase and
RT phosphoglycerate kinase in Chinese hamster ovary cell line CHO-K1 and
RT identification of defects in R1.1.7, a glycolysis-deficient variant of CHO-
RT K1.";
RL Somat. Cell Mol. Genet. 21:75-81(1995).
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:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; Z37974; CAA86028.1; -; mRNA.
DR PIR; I48074; I48074.
DR RefSeq; NP_001233654.1; NM_001246725.1.
DR AlphaFoldDB; P50310; -.
DR SMR; P50310; -.
DR STRING; 10029.NP_001233654.1; -.
DR PRIDE; P50310; -.
DR Ensembl; ENSCGRT00001007008; ENSCGRP00001004651; ENSCGRG00001005933.
DR GeneID; 100689467; -.
DR KEGG; cge:100689467; -.
DR CTD; 5230; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR OrthoDB; 838642at2759; -.
DR UniPathway; UPA00109; UER00185.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Glycolysis; Hydroxylation; Kinase;
KW Nucleotide-binding; Phosphoprotein; 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_0000145828"
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; 44563 MW; 88649100C59FDE05 CRC64;
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV GPEVENACAN PAAGTVILLE
NLRFHVEEEG KGKDASGNKI KAEPAKIDAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
AFTFLKVLNN MEIGTSLYDE EGAKIVKDLM AKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
ATVASGIPAG WMGLDCGTES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR GTKSLMDEVV
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV
