ID PGK_STRP2 Reviewed; 398 AA. AC Q04LZ5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 95. 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=SPD_0445; OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=373153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D39 / NCTC 7466; RX PubMed=17041037; DOI=10.1128/jb.01148-06; RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.; RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus RT pneumoniae and comparison with that of unencapsulated laboratory strain RT R6."; RL J. Bacteriol. 189:38-51(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; CP000410; ABJ54881.1; -; Genomic_DNA. DR RefSeq; WP_001096759.1; NZ_JAMLJR010000009.1. DR PDB; 3ZLB; X-ray; 1.78 A; A=1-398. DR PDBsum; 3ZLB; -. DR AlphaFoldDB; Q04LZ5; -. DR SMR; Q04LZ5; -. DR PaxDb; 373153-SPD_0445; -. DR KEGG; spd:SPD_0445; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_1_9; -. DR BioCyc; SPNE373153:G1G6V-486-MONOMER; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000001452; Chromosome. DR GO; GO:0009986; C:cell surface; IDA:CAFA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CAFA. DR GO; GO:0043532; F:angiostatin binding; IPI:CAFA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0002020; F:protease binding; IPI:CAFA. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051919; P:positive regulation of fibrinolysis; IPI:CAFA. DR GO; GO:0010756; P:positive regulation of plasminogen activation; IPI:CAFA. 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..398 FT /note="Phosphoglycerate kinase" FT /id="PRO_1000009654" FT BINDING 21..23 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 59..62 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 157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145" FT BINDING 327 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" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 15..19 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 35..49 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 75..85 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 98..105 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:3ZLB" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:3ZLB" FT TURN 127..131 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 133..141 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:3ZLB" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 169..174 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:3ZLB" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 209..218 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 228..235 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 270..278 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 301..311 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 315..321 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 333..343 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 355..363 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 367..369 FT /evidence="ECO:0007829|PDB:3ZLB" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 378..384 FT /evidence="ECO:0007829|PDB:3ZLB" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:3ZLB" SQ SEQUENCE 398 AA; 41939 MW; BDDA8FD4B336BC91 CRC64; MAKLTVKDVD LKGKKVLVRV DFNVPLKDGV ITNDNRITAA LPTIKYIIEQ GGRAILFSHL GRVKEESDKA GKSLAPVAAD LAAKLGQDVV FPGVTRGAEL EAAINALEDG QVLLVENTRY EDVDGKKESK NDPELGKYWA SLGDGIFVND AFGTAHRAHA SNVGISANVE KAVAGFLLEN EIAYIQEAVE TPERPFVAIL GGSKVSDKIG VIENLLEKAD KVLIGGGMTY TFYKAQGIEI GNSLVEEDKL DVAKALLEKA NGKLILPVDS KEANAFAGYT EVRDTEGEAV SEGFLGLDIG PKSIAKFDEA LTGAKTVVWN GPMGVFENPD FQAGTIGVMD AIVKQPGVKS IIGGGDSAAA AINLGRADKF SWISTGGGAS MELLEGKVLP GLAALTEK //