ID   PGK_DICDI               Reviewed;         420 AA.
AC   Q9GPM4; Q54K34;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgkA {ECO:0000312|EMBL:AAG34561.2}; ORFNames=DDB_G0287595;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG34561.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CALMODULIN.
RX   PubMed=15363631; DOI=10.1016/j.bbamcr.2004.08.003;
RA   Myre M.A., O'Day D.H.;
RT   "Calmodulin binds to and inhibits the activity of phosphoglycerate
RT   kinase.";
RL   Biochim. Biophys. Acta 1693:177-183(2004).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:EAL63606.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000269|PubMed:15875012};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA   Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA   Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA   Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT   "A transcriptional profile of multicellular development in Dictyostelium
RT   discoideum.";
RL   Development 129:1543-1552(2002).
RN   [4] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA   Iranfar N., Fuller D., Loomis W.F.;
RT   "Genome-wide expression analyses of gene regulation during early
RT   development of Dictyostelium discoideum.";
RL   Eukaryot. Cell 2:664-670(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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. Interacts with calmodulin in the presence of Ca(2+).
CC       {ECO:0000250|UniProtKB:P00558, ECO:0000269|PubMed:15363631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00558}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development. Expression levels
CC       decrease steadily from the initiation of development until culmination.
CC       Levels increase after 18 hours of development and peak at 22 hours,
CC       after which they decrease again. {ECO:0000269|PubMed:11923193,
CC       ECO:0000269|PubMed:12912885}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000255}.
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DR   EMBL; AF316577; AAG34561.2; -; mRNA.
DR   EMBL; AAFI02000103; EAL63606.1; -; Genomic_DNA.
DR   RefSeq; XP_637130.1; XM_632038.1.
DR   AlphaFoldDB; Q9GPM4; -.
DR   SMR; Q9GPM4; -.
DR   STRING; 44689.Q9GPM4; -.
DR   PaxDb; 44689-DDB0191349; -.
DR   EnsemblProtists; EAL63606; EAL63606; DDB_G0287595.
DR   GeneID; 8626225; -.
DR   KEGG; ddi:DDB_G0287595; -.
DR   dictyBase; DDB_G0287595; pgkA.
DR   eggNOG; KOG1367; Eukaryota.
DR   HOGENOM; CLU_025427_0_2_1; -.
DR   InParanoid; Q9GPM4; -.
DR   OMA; DMIFDIG; -.
DR   PhylomeDB; Q9GPM4; -.
DR   Reactome; R-DDI-70171; Glycolysis.
DR   Reactome; R-DDI-70263; Gluconeogenesis.
DR   UniPathway; UPA00109; UER00185.
DR   PRO; PR:Q9GPM4; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IC:dictyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IDA:dictyBase.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:dictyBase.
DR   GO; GO:0006094; P:gluconeogenesis; ISS:dictyBase.
DR   GO; GO:0006096; P:glycolytic process; ISS:dictyBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 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:SF0; PHOSPHOGLYCERATE KINASE; 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.
PE   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Cytoplasm; Glycolysis; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..420
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000293630"
FT   REGION          209..228
FT                   /note="Calmodulin binding"
FT                   /evidence="ECO:0000269|PubMed:15363631"
FT   BINDING         27..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         67..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   BINDING         376..379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         199
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00558,
FT                   ECO:0000250|UniProtKB:P09411"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09411"
SQ   SEQUENCE   420 AA;  45709 MW;  6FEA000CF9B5F83E CRC64;
     MSSNKIGNKL SLDKVDVKGK RVLIRVDYNV PLDKNNNITS TQRIDASIPT LEYCLKNGAK
     SIVLMSHLGR PDGLVKPEYS LKPVVKVLED QLKRPIKFLS DCVGEQVEKE CANPEEGTVI
     LLENLRFHIE EEGSGVDAEG KKVKANPEKV KEFRESLTKL GDVYVNDAFG TAHRAHSSMV
     GINLPQKAAG FLMKKELEYF AKALESPSKP FLAILGGAKV SDKIKLIENL LYKVDEMIIG
     GGMAFTFKKF IDNKEIGSSL FEKTAEQITK DIIAKAAKNN VKLHFPVDYV IADKFDNDAN
     IKTVTQDQGI PEGWMGLDCG PETIKENRDT ISRAKTIVWN GPMGVFEKSN FEAGTKAAMD
     DVVNATTNGA ITIIGGGDTA TCAAKYNTED KVSHVSTGGG ASLELLEGKE LPGVTALSDL
//