ID R4R368_9SOLA Unreviewed; 361 AA. AC R4R368; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 25-MAY-2022, entry version 20. DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532}; DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532}; DE Flags: Fragment; GN Name=PGK {ECO:0000313|EMBL:AGL76992.1}; OS Anisodus luridus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; OC Anisodus. OX NCBI_TaxID=258458 {ECO:0000313|EMBL:AGL76992.1}; RN [1] {ECO:0000313|EMBL:AGL76992.1} RP NUCLEOTIDE SEQUENCE. RA Qin B., Ma L., Liao Z.; RL Submitted (MAR-2013) 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 Evidence={ECO:0000256|RuleBase:RU000532}; CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}. 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; KC713803; AGL76992.1; -; mRNA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; SSF53748; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724- KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}. FT NP_BIND 342..345 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2" FT REGION 10..12 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1" FT REGION 49..52 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 26 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 107 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 140 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1" FT BINDING 191 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2" FT BINDING 313 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGL76992.1" FT NON_TER 361 FT /evidence="ECO:0000313|EMBL:AGL76992.1" SQ SEQUENCE 361 AA; 38505 MW; DE9149DBCBE9DFAF CRC64; KGKRVFVRVD LNVPLDDNFN ITDDTRIRAA LPTINYLMQN GARVILASHL GRPKGVTPKY SLKPLVPRLS ELLGLEVKMA NDSVGPEVEK LVAELPEGGV LLLENVRFYK EEEKNEPEFA KKLASLADLY VNDAFGTAHR AHASTEGVAK VLKPAVAGFL MQKELDYLVG AVSNPQKPFA AIVGGSEVSS KIGVIESLLE KVDVLLLGGG MIFTFYKAQG YAVGSSLVEE DKLDLATSLM EKAKTKGVSL LLPTDVVIAD KFAADANSKI VPASEIPDDW MGLDIGPDAI KSFGSALDTT KTIIWNGPMG VFEFDKFAAG TEAIAHKLAE LSGKGVTTII GGGDSVAAVE KVGLAEKMSH I //