ID PGK_DEIRA Reviewed; 411 AA. AC Q9RUP2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 124. 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=DR_1342; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=243230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / RC NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans RT R1."; RL Science 286:1571-1577(1999). 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 -!- 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; AE000513; AAF10913.1; -; Genomic_DNA. DR PIR; D75408; D75408. DR RefSeq; NP_295065.1; NC_001263.1. DR AlphaFoldDB; Q9RUP2; -. DR SMR; Q9RUP2; -. DR STRING; 243230.DR_1342; -. DR PaxDb; 243230-DR_1342; -. DR EnsemblBacteria; AAF10913; AAF10913; DR_1342. DR KEGG; dra:DR_1342; -. DR PATRIC; fig|243230.17.peg.1539; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_2_0; -. DR InParanoid; Q9RUP2; -. DR OrthoDB; 9808460at2; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000002524; Chromosome I. 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 CDD; cd00318; Phosphoglycerate_kinase; 1. 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..411 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000145939" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 41..43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 79..82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 310 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 341 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 369..372 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" SQ SEQUENCE 411 AA; 42899 MW; 39407D5EC7E34D37 CRC64; MTGLCPLHQP SPLDHPHSGG TPMQNLSQLD VKGKRVLVRV DYNVPVGDGV VQDDTRITAS VPTIKKLLDG GASVVLMSHF GRPKNGPEDK YSLKPVAEAV SRALGQDVKF IPSLPGSDET LQAVQALRPG EVALLENVRF EAGEEKNDAA LNDKLAKLGD AFVLDAFGSA HRAHSSVSGV AGKLPHAAGG LLQSEVDALG KLLHAPEHPY VVIIGGAKVS DKIKVIENLL PKVDRMLIGG GMMFTFIKAR GGQIGNSLVE DDQLDLAKGL LEKYGDKLLL PTDAVAADKF AADAQSKVVP ADQIPDGWMG LDIGPDTQRA YADALQGAKT VFWNGPMGVF EFDQFAAGTN AVAAAVGSLK DQAYTVVGGG DSVSAINKSG KADQIDHIST GGGASLELLE GKELPGVVAM A //