PGK_DICDI
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 03-AUG-2022, entry version 119.
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 (Slime mold).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.DDB0191349; -.
DR PaxDb; Q9GPM4; -.
DR PRIDE; Q9GPM4; -.
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; YVNDAYS; -.
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 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 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
