ID A0A9C9PKV8_9GAMM Unreviewed; 394 AA. AC A0A9C9PKV8; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 13-SEP-2023, entry version 3. DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145}; DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145}; GN Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145}; GN ORFNames=ENF37_02655 {ECO:0000313|EMBL:HEW97531.1}; OS Beggiatoa sp. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Beggiatoa. OX NCBI_TaxID=1962953 {ECO:0000313|EMBL:HEW97531.1, ECO:0000313|Proteomes:UP000885946}; RN [1] {ECO:0000313|EMBL:HEW97531.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HyVt-12 {ECO:0000313|EMBL:HEW97531.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-e00719(2020). 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:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP- CC Rule:MF_00145, ECO:0000256|RuleBase:RU000532}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_00145}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HEW97531.1}. 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; DQWX01000089; HEW97531.1; -; Genomic_DNA. DR Proteomes; UP000885946; Unassembled WGS sequence. 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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00145}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00145}. FT BINDING 21..23 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 59..62 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-2" FT BINDING 322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-2" FT BINDING 348..351 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145, FT ECO:0000256|PIRSR:PIRSR000724-2" SQ SEQUENCE 394 AA; 41353 MW; A8A431CB71F62CE5 CRC64; MPIIKMTDLD LKGKRVLIRE DLNVPLKDGK VASDVRIKAS LPTIKHAMEA GAKVSLMSHL GRPKEGEFDP KASLAPVAEH LEKLLGKPVK LVKNWLDGID MADGEVVLCE NVRFNKGEKK NDDELSKKMA ALCDVYVMDA FGTAHRAQAS THGVAKYAPV ACAGPLLAGE LEALGKALDN PARPMVAIVG GSKVSTKLTV LESLSKVVDQ LIVGGGIANT FIAAAGHNVG KSLYEADLIE EASKLTAAAQ ARGGEIPVPT DIVVGTVSPF EQADAKATLK AVDEATDDEM IFDVGPDTSA KFAEILKKAG TIVWNGPVGV FEYDQFGAGT KALSEAIAES SAFSIAGGGD TLAAVDKYGV IKQVSYISTG GGAFLEFLEG KKLPAVDILE ERGN //