ID PGK_PRIM3 Reviewed; 394 AA. AC P24269; D5DNB0; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=BMD_5037; OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=592022; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2123031; DOI=10.1093/nar/18.21.6423; RA Schlaepfer B.S., Branlant C., Branlant G., Zuber H.; RT "Nucleotide sequence of the phosphoglycerate kinase gene from Bacillus RT megaterium."; RL Nucleic Acids Res. 18:6423-6423(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1452037; DOI=10.1016/0378-1119(92)90031-j; RA Schlaepfer B.S., Zuber H.; RT "Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate RT dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap RT operon) from mesophilic Bacillus megaterium: comparison with corresponding RT sequences from thermophilic Bacillus stearothermophilus."; RL Gene 122:53-62(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 / IMG 1521; RX PubMed=21705586; DOI=10.1128/jb.00449-11; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S., RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C., RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J., RA Bremer E., Jahn D., Ravel J., Vary P.S.; RT "Genome sequences of the biotechnologically important Bacillus megaterium RT strains QM B1551 and DSM319."; RL J. Bacteriol. 193:4199-4213(2011). 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {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; X54519; CAA38375.1; -; Genomic_DNA. DR EMBL; M87647; AAA73203.1; -; Genomic_DNA. DR EMBL; M87648; AAA73206.1; -; Genomic_DNA. DR EMBL; CP001982; ADF41837.1; -; Genomic_DNA. DR PIR; S13125; KIBSGM. DR RefSeq; WP_013059701.1; NZ_CP120609.1. DR AlphaFoldDB; P24269; -. DR SMR; P24269; -. DR GeneID; 64144493; -. DR KEGG; bmd:BMD_5037; -. DR HOGENOM; CLU_025427_0_2_9; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000002365; Chromosome. 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 Phosphoprotein; Transferase. FT CHAIN 1..394 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000145903" FT BINDING 21..23 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 59..62 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 151 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 323 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 350..353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000250" FT MOD_RES 299 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" SQ SEQUENCE 394 AA; 42457 MW; 7A2E6B978FA7008B CRC64; MNKKTLKDID VKGKRVFCRV DFNVPMKDGK VTDETRIRAA IPTIQYLVEQ GAKVILASHL GRPKGEVVEE LRLNAVAERL QALLGKDVAK ADEAFGEEVK KTIDGMSEGD VLVLENVRFY PGEEKNDPEL AKAFAELADV YVNDAFGAAH RAHASTEGIA QHIPAVAGFL MEKELDVLSK ALSNPERPFT AIVGGAKVKD KIGVIDHLLD KVDNLIIGGG LSYTFIKALG HEVGKSLLEE DKIELAKSFM EKAKKNGVNF YMPVDVVVAD DFSNDANIQV VSIEDIPSDW EGLDAGPKTR EIYADVIKNS KLVIWNGPMG VFELDAFANG TKAVAEALAE ATDTYSVIGG GDSAAAVEKF NLADKMSHIS TGGGASLEFM EGKELPGVVA LNDK //