ID PGK_CHLCH Reviewed; 397 AA. AC Q3ANU2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Cag_0044; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000108; ABB27323.1; -; Genomic_DNA. DR AlphaFoldDB; Q3ANU2; -. DR SMR; Q3ANU2; -. DR STRING; 340177.Cag_0044; -. DR KEGG; cch:Cag_0044; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_2_10; -. DR OrthoDB; 9808460at2; -. DR UniPathway; UPA00109; UER00185. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. 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 Transferase. FT CHAIN 1..397 FT /note="Phosphoglycerate kinase" FT /id="PRO_1000057975" FT BINDING 21..23 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 37 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 60..63 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 152 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 294 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 325 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 397 AA; 42082 MW; F3C5E607D32A88C0 CRC64; MEKKTLSDIA TQGKRVLMRV DFNVPLDENK NITDDKRIVE SLPSIRKVIE EGGRLILMSH LGRPKGKVNA EFSLAPVAAR LSELLDCPVG MAKDCIGTEV MQQVLALQDG EVLLLENLRF HAEEEANDAD FAKELASLGE IYVNDAFGTA HRAHASTEGI THYVQTAVAG FLIERELRYL GKALQEPERP FVAILGGSKI SGKIDVLENL FKKVDTVLIG GAMVFTFFKA QGYEVGKSLV EESKIELALS ILEQAKAKGI KLLLPTDVVV TAEISADAES SVASIADMPN NLIGVDIGPE TAAAYRNEII GARTVLWNGP MGVFELDNFA TGTIAVAQAL ADATAQGATT IVGGGDSAAA IAKAGLASEI THISTGGGAS LEFLEGKELP GIAALNN //