ID   PGK_CAEEL               Reviewed;         417 AA.
AC   P91427;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Probable phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk-1; ORFNames=T03F1.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; FO080917; CCD67788.1; -; Genomic_DNA.
DR   PIR; T29198; T29198.
DR   RefSeq; NP_491245.1; NM_058844.4.
DR   AlphaFoldDB; P91427; -.
DR   SMR; P91427; -.
DR   BioGRID; 37439; 19.
DR   IntAct; P91427; 1.
DR   MINT; P91427; -.
DR   STRING; 6239.T03F1.3; -.
DR   iPTMnet; P91427; -.
DR   World-2DPAGE; 0020:P91427; -.
DR   EPD; P91427; -.
DR   PaxDb; P91427; -.
DR   PeptideAtlas; P91427; -.
DR   EnsemblMetazoa; T03F1.3.1; T03F1.3.1; WBGene00020185.
DR   GeneID; 171965; -.
DR   KEGG; cel:CELE_T03F1.3; -.
DR   UCSC; T03F1.3; c. elegans.
DR   CTD; 171965; -.
DR   WormBase; T03F1.3; CE13100; WBGene00020185; pgk-1.
DR   eggNOG; KOG1367; Eukaryota.
DR   GeneTree; ENSGT00390000008820; -.
DR   HOGENOM; CLU_025427_0_0_1; -.
DR   InParanoid; P91427; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 838642at2759; -.
DR   PhylomeDB; P91427; -.
DR   Reactome; R-CEL-70171; Glycolysis.
DR   Reactome; R-CEL-70263; Gluconeogenesis.
DR   UniPathway; UPA00109; UER00185.
DR   PRO; PR:P91427; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00020185; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..417
FT                   /note="Probable phosphoglycerate kinase"
FT                   /id="PRO_0000145844"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  44113 MW;  CB0369287AFE5AC4 CRC64;
     MSSLNKLAID QLNLAGKRVL IRVDFNVPLK DGKITNNQRI AAAVPTIQHA LSNGAKSVVL
     MSHLGRPDGR RQDKYTLKPV AEELKALLKK DVLFLDDCVG SEVEAACADP APGSVILLEN
     LRYHLEEEGK GVDASGAKVK ADSAAVKKFR ESLTKLGDIY VNDAFGTAHR AHSSMVGVEH
     SQRASGFLLK NELSYFSKAL DNPARPFLAI LGGAKVADKI QLIKNLLDKV NEMIIGGGMA
     YTFLKVAQGV KIGNSLYDEE GAKIVNELLE AAKAKGVQIH LPVDFVIADK FAEDATSKTV
     TAEEGVPDGH MGLDVGPESS KIFAAAIQRA KTIVWNGPAG VFEFDKFATG TKSLMDEVVK
     ATAAGAITII GGGDTATAAK KYNTEDKVSH VSTGGGASLE LLEGKVLPGV DALSPAQ