ID PGK_STRR6 Reviewed; 398 AA. AC Q8DQX8; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145}; DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145}; GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=spr0441; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). RN [2] RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x; RA Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A., RA Echenique J., Trombe M.C., Branny P.; RT "Characterization of a eukaryotic type serine/threonine protein kinase and RT protein phosphatase of Streptococcus pneumoniae and identification of RT kinase substrates."; RL FEBS J. 272:1243-1254(2005). 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:0000255|HAMAP-Rule:MF_00145}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_00145}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15720398}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00145}. 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; AE007317; AAK99245.1; -; Genomic_DNA. DR PIR; A97927; A97927. DR RefSeq; NP_358035.1; NC_003098.1. DR RefSeq; WP_001096759.1; NC_003098.1. DR AlphaFoldDB; Q8DQX8; -. DR SMR; Q8DQX8; -. DR STRING; 171101.spr0441; -. DR MoonProt; Q8DQX8; -. DR KEGG; spr:spr0441; -. DR PATRIC; fig|171101.6.peg.487; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_1_9; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000586; Chromosome. 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; IBA:GO_Central. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central. 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; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2. 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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..398 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000146016" FT BINDING 21..23 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 59..62 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 327 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 354..357 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" SQ SEQUENCE 398 AA; 41939 MW; BDDA8FD4B336BC91 CRC64; MAKLTVKDVD LKGKKVLVRV DFNVPLKDGV ITNDNRITAA LPTIKYIIEQ GGRAILFSHL GRVKEESDKA GKSLAPVAAD LAAKLGQDVV FPGVTRGAEL EAAINALEDG QVLLVENTRY EDVDGKKESK NDPELGKYWA SLGDGIFVND AFGTAHRAHA SNVGISANVE KAVAGFLLEN EIAYIQEAVE TPERPFVAIL GGSKVSDKIG VIENLLEKAD KVLIGGGMTY TFYKAQGIEI GNSLVEEDKL DVAKALLEKA NGKLILPVDS KEANAFAGYT EVRDTEGEAV SEGFLGLDIG PKSIAKFDEA LTGAKTVVWN GPMGVFENPD FQAGTIGVMD AIVKQPGVKS IIGGGDSAAA AINLGRADKF SWISTGGGAS MELLEGKVLP GLAALTEK //