ID PGK_THET8 Reviewed; 390 AA. AC P09403; Q5SJV2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 150. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=TTHA0906; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=3052437; DOI=10.1042/bj2540509; RA Bowen D., Littlechild J.A., Fothergill J.E., Watson H.C., Hall L.; RT "Nucleotide sequence of the phosphoglycerate kinase gene from the extreme RT thermophile Thermus thermophilus. Comparison of the deduced amino acid RT sequence with that of the mesophilic yeast phosphoglycerate kinase."; RL Biochem. J. 254:509-517(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) 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 -!- 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; X12464; CAA31006.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70729.1; -; Genomic_DNA. DR RefSeq; WP_011228285.1; NC_006461.1. DR PDB; 1V6S; X-ray; 1.50 A; A/B=1-390. DR AlphaFoldDB; P09403; -. DR SMR; P09403; -. DR EnsemblBacteria; BAD70729; BAD70729; BAD70729. DR GeneID; 3169950; -. DR KEGG; ttj:TTHA0906; -. DR PATRIC; fig|300852.9.peg.898; -. DR eggNOG; COG0126; Bacteria. DR HOGENOM; CLU_025427_0_2_0; -. DR PhylomeDB; P09403; -. DR BRENDA; 2.7.2.3; 2305. DR UniPathway; UPA00109; UER00185. DR EvolutionaryTrace; P09403; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:TreeGrafter. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:TreeGrafter. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR FunFam; 3.40.50.1260:FF:000003; Phosphoglycerate kinase; 1. DR FunFam; 3.40.50.1260:FF:000006; 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. DR PDBsum; 1V6S; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; KW Glycolysis; Kinase; Nucleotide-binding; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..390 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000146027" FT BINDING 19..21 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 34 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 57..60 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 347..350 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 33..47 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 94..101 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1V6S" FT TURN 118..123 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 151..155 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 166..176 FT /evidence="ECO:0007829|PDB:1V6S" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 199..205 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 210..214 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 219..225 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 240..253 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 261..268 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 288..292 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:1V6S" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:1V6S" FT TURN 322..325 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 326..336 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 342..347 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 348..355 FT /evidence="ECO:0007829|PDB:1V6S" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 363..366 FT /evidence="ECO:0007829|PDB:1V6S" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 372..379 FT /evidence="ECO:0007829|PDB:1V6S" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:1V6S" SQ SEQUENCE 390 AA; 41777 MW; 3829E89FCEDC90B3 CRC64; MRTLLDLDPK GKRVLVRVDY NVPVQDGKVQ DETRILESLP TLRHLLAGGA SLVLLSHLGR PKGPDPKYSL APVGEALRAH LPEARFAPFP PGSEEARREA EALRPGEVLL LENVRFEPGE EKNDPELSAR YARLGEAFVL DAFGSAHRAH ASVVGVARLL PAYAGFLMEK EVRALSRLLK DPERPYAVVL GGAKVSDKIG VIESLLPRID RLLIGGAMAF TFLKALGGEV GRSLVEEDRL DLAKDLLGRA EALGVRVYLP EDVVAAERIE AGVETRVFPA RAIPVPYMGL DIGPKTREAF ARALEGARTV FWNGPMGVFE VPPFDEGTLA VGQAIAALEG AFTVVGGGDS VAAVNRLGLK ERFGHVSTGG GASLEFLEKG TLPGLEVLEG //