ID PGK_CLOBH Reviewed; 398 AA. AC A5HYC0; A7FZK4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 87. 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=CBO0227, CLC_0283; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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; CP000727; ABS39087.1; -; Genomic_DNA. DR EMBL; AM412317; CAL81779.1; -; Genomic_DNA. DR RefSeq; WP_011948027.1; NC_009698.1. DR RefSeq; YP_001252771.1; NC_009495.1. DR RefSeq; YP_001386183.1; NC_009698.1. DR AlphaFoldDB; A5HYC0; -. DR SMR; A5HYC0; -. DR GeneID; 5187988; -. DR KEGG; cbh:CLC_0283; -. DR KEGG; cbo:CBO0227; -. DR PATRIC; fig|413999.7.peg.225; -. DR HOGENOM; CLU_025427_0_2_9; -. DR UniPathway; UPA00109; UER00185. DR PRO; PR:A5HYC0; -. DR Proteomes; UP000001986; 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 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..398 FT /note="Phosphoglycerate kinase" FT /id="PRO_1000009607" FT BINDING 23..25 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 38 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 61..64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 297 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 328 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; 43062 MW; D2092EB5B08046A8 CRC64; MNYNKKSIED IDVKGKKVLV RCDFNVPLNE GKITDENRLV GALPTIKYLM EKGAKIILCS HMGKPKGEPK KELSLLPVAK RLSEMLNKEV IFADDDNVVG ENAKKAVEDM KDGDVVLLQN TRYRKEETKN EEVFSKELAS LADVFVNDAF GTAHRAHCST VGVTNYLKEA ACGYLIQKEL KFLGNAVEKP ERPFVAILGG AKVSDKINVI NNLLDKVDTL IIGGGMGYTF LKAQGYTIGN SLVEEDKVEY SKEMIDKAKE KGVNLLLPID NVVADKFDKD ASPVITEDQN IGEGYMGLDI GPKTAKIYSD AIKSAKTVVW NGPMGVFEFK SFANGTIEVA KAMADSDAVT IIGGGDSAAA VNILGFGDKM THISTGGGAS LEFLEGKELP GIAALNDK //