ID PGK_COXBU Reviewed; 391 AA. AC Q83AU6; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 109. 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}; GN OrderedLocusNames=CBU_1782; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). 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 -!- SEQUENCE CAUTION: CC Sequence=AAO91276.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE016828; AAO91276.2; ALT_INIT; Genomic_DNA. DR RefSeq; NP_820762.2; NC_002971.3. DR PDB; 4NG4; X-ray; 2.78 A; A/B/C=1-388. DR PDBsum; 4NG4; -. DR AlphaFoldDB; Q83AU6; -. DR SMR; Q83AU6; -. DR STRING; 227377.CBU_1782; -. DR DNASU; 1209693; -. DR EnsemblBacteria; AAO91276; AAO91276; CBU_1782. DR GeneID; 1209693; -. DR KEGG; cbu:CBU_1782; -. DR PATRIC; fig|227377.7.peg.1769; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_2_6; -. DR OrthoDB; 9808460at2; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000002671; 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 3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..391 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000145938" FT BINDING 16..18 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 31 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 54..57 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 314 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 340..343 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT HELIX 1..3 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 30..44 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 70..78 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:4NG4" FT TURN 111..116 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 118..126 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:4NG4" FT TURN 144..147 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 148..152 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 154..158 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 160..174 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 211..219 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 234..247 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 255..262 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 302..308 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 320..331 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 334..338 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 341..349 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:4NG4" FT STRAND 356..359 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 364..371 FT /evidence="ECO:0007829|PDB:4NG4" FT HELIX 376..385 FT /evidence="ECO:0007829|PDB:4NG4" SQ SEQUENCE 391 AA; 42363 MW; A569E166D68D5ADE CRC64; MSNLNLHNKR VMIREDLNVP MKNGKITNDE RIVRALPTIQ KAIEQKARVM ILSHLGRPEE GKFEKEFSLA PVARLLSKKL NQKVPLINDW LKGVAVEPGQ AILCENVRFN KGENENNTEL AKRMAELCDI FVMDAFATAH RAQASTAGVA AYAKLACAGP LLISEVEALS RALENPQKPL VAVVGGSKVS TKIHLLENLL DKVDQLIVGG GIANTFLKAQ GYSIGKSLCE NEWLDAAQQF WEKAAEKNVS LPLPVDVIVA DELSEDAKAT VKNIDAVTSN ESIFDVGPNT SATYAKLMAQ AGTIVWNGPI GVFEIEAFSQ GTRALAQAVA KSTAYSIVGG GDTLAALDKF NLTDQMSYVS TAGGAFLEFL EGKILPAIKI LTQRAKEYEQ K //